Structural basis for the binding of DNP and purine nucleotides onto UCP1

Uncoupling protein 1 (UCP1) conducts protons through the inner mitochondrial membrane to uncouple mitochondrial respiration from ATP production, thereby converting the electrochemical gradient of protons into heat 1 , 2 . The activity of UCP1 is activated by endogenous fatty acids and synthetic smal...

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Published in:	Nature (London) Vol. 620; no. 7972; pp. 226 - 231
Main Authors:	Kang, Yunlu, Chen, Lei
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 03.08.2023 Nature Publishing Group
Subjects:	101/28 2,4-Dinitrophenol 2,4-Dinitrophenol - chemistry 2,4-Dinitrophenol - metabolism 631/45/612/1237 631/535/1258/1259 82/80 82/83 Adenosine triphosphate Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism ATP Binding sites Cell Membrane - metabolism Cytosol - metabolism Electrochemistry Electron transport Fatty acids Fatty Acids - metabolism Humanities and Social Sciences Humans Lipids multidisciplinary Nucleotides Permeability Protein Conformation Proteins Protons Respiration Science Science (multidisciplinary) Uncoupling protein 1 Uncoupling Protein 1 - chemistry Uncoupling Protein 1 - metabolism
ISSN:	0028-0836, 1476-4687, 1476-4687
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Abstract	Uncoupling protein 1 (UCP1) conducts protons through the inner mitochondrial membrane to uncouple mitochondrial respiration from ATP production, thereby converting the electrochemical gradient of protons into heat 1 , 2 . The activity of UCP1 is activated by endogenous fatty acids and synthetic small molecules, such as 2,4-dinitrophenol (DNP), and is inhibited by purine nucleotides, such as ATP 3 – 5 . However, the mechanism by which UCP1 binds to these ligands remains unknown. Here we present the structures of human UCP1 in the nucleotide-free state, the DNP-bound state and the ATP-bound state. The structures show that the central cavity of UCP1 is open to the cytosolic side. DNP binds inside the cavity, making contact with transmembrane helix 2 (TM2) and TM6. ATP binds in the same cavity and induces conformational changes in TM2, together with the inward bending of TM1, TM4, TM5 and TM6 of UCP1, resulting in a more compact structure of UCP1. The binding site of ATP overlaps with that of DNP, suggesting that ATP competitively blocks the functional engagement of DNP, resulting in the inhibition of the proton-conducting activity of UCP1. Using cryo-electron microscopy, the structures of human UCP1 in the nucleotide-free state, the DNP activator-bound state, and the inhibitory ATP-bound state are resolved, providing details of how purine nucleotides inhibit UCP1.
AbstractList	Uncoupling protein 1 (UCP1) conducts protons through the inner mitochondrial membrane to uncouple mitochondrial respiration from ATP production, thereby converting the electrochemical gradient of protons into heat. The activity of UCP1 is activated by endogenous fatty acids and synthetic small molecules, such as 2,4-dinitrophenol (DNP), and is inhibited by purine nucleotides, such as ATP. However, the mechanism by which UCP1 binds to these ligands remains unknown. Here we present the structures of human UCP1 in the nucleotide-free state, the DNP-bound state and the ATP-bound state. The structures show that the central cavity of UCP1 is open to the cytosolic side. DNP binds inside the cavity, making contact with transmembrane helix 2 (TM2) and TM6. ATP binds in the same cavity and induces conformational changes in TM2, together with the inward bending of TM1, TM4, TM5 and TM6 of UCP1, resulting in a more compact structure of UCP1. The binding site of ATP overlaps with that of DNP, suggesting that ATP competitively blocks the functional engagement of DNP, resulting in the inhibition of the proton-conducting activity of UCP1. Uncoupling protein 1 (UCP1) conducts protons through the inner mitochondrial membrane to uncouple mitochondrial respiration from ATP production, thereby converting the electrochemical gradient of protons into heat1,2. The activity of UCP1 is activated by endogenous fatty acids and synthetic small molecules, such as 2,4-dinitrophenol (DNP), and is inhibited by purine nucleotides, such as ATP3-5. However, the mechanism by which UCP1 binds to these ligands remains unknown. Here we present the structures of human UCP1 in the nucleotide-free state, the DNP-bound state and the ATP-bound state. The structures show that the central cavity of UCP1 is open to the cytosolic side. DNP binds inside the cavity, making contact with transmembrane helix 2 (TM2) and TM6. ATP binds in the same cavity and induces conformational changes in TM2, together with the inward bending of TM1, TM4, TM5 and TM6 of UCP1, resulting in a more compact structure of UCP1. The binding site of ATP overlaps with that of DNP, suggesting that ATP competitively blocks the functional engagement of DNP, resulting in the inhibition of the proton-conducting activity of UCP1.Uncoupling protein 1 (UCP1) conducts protons through the inner mitochondrial membrane to uncouple mitochondrial respiration from ATP production, thereby converting the electrochemical gradient of protons into heat1,2. The activity of UCP1 is activated by endogenous fatty acids and synthetic small molecules, such as 2,4-dinitrophenol (DNP), and is inhibited by purine nucleotides, such as ATP3-5. However, the mechanism by which UCP1 binds to these ligands remains unknown. Here we present the structures of human UCP1 in the nucleotide-free state, the DNP-bound state and the ATP-bound state. The structures show that the central cavity of UCP1 is open to the cytosolic side. DNP binds inside the cavity, making contact with transmembrane helix 2 (TM2) and TM6. ATP binds in the same cavity and induces conformational changes in TM2, together with the inward bending of TM1, TM4, TM5 and TM6 of UCP1, resulting in a more compact structure of UCP1. The binding site of ATP overlaps with that of DNP, suggesting that ATP competitively blocks the functional engagement of DNP, resulting in the inhibition of the proton-conducting activity of UCP1. Uncoupling protein 1 (UCP1) conducts protons through the inner mitochondrial membrane to uncouple mitochondrial respiration from ATP production, thereby converting the electrochemical gradient of protons into heat 1 , 2 . The activity of UCP1 is activated by endogenous fatty acids and synthetic small molecules, such as 2,4-dinitrophenol (DNP), and is inhibited by purine nucleotides, such as ATP 3 – 5 . However, the mechanism by which UCP1 binds to these ligands remains unknown. Here we present the structures of human UCP1 in the nucleotide-free state, the DNP-bound state and the ATP-bound state. The structures show that the central cavity of UCP1 is open to the cytosolic side. DNP binds inside the cavity, making contact with transmembrane helix 2 (TM2) and TM6. ATP binds in the same cavity and induces conformational changes in TM2, together with the inward bending of TM1, TM4, TM5 and TM6 of UCP1, resulting in a more compact structure of UCP1. The binding site of ATP overlaps with that of DNP, suggesting that ATP competitively blocks the functional engagement of DNP, resulting in the inhibition of the proton-conducting activity of UCP1. Using cryo-electron microscopy, the structures of human UCP1 in the nucleotide-free state, the DNP activator-bound state, and the inhibitory ATP-bound state are resolved, providing details of how purine nucleotides inhibit UCP1. Uncoupling protein 1 (UCP1) conducts protons through the inner mitochondrial membrane to uncouple mitochondrial respiration from ATP production, thereby converting the electrochemical gradient of protons into heat . The activity of UCP1 is activated by endogenous fatty acids and synthetic small molecules, such as 2,4-dinitrophenol (DNP), and is inhibited by purine nucleotides, such as ATP . However, the mechanism by which UCP1 binds to these ligands remains unknown. Here we present the structures of human UCP1 in the nucleotide-free state, the DNP-bound state and the ATP-bound state. The structures show that the central cavity of UCP1 is open to the cytosolic side. DNP binds inside the cavity, making contact with transmembrane helix 2 (TM2) and TM6. ATP binds in the same cavity and induces conformational changes in TM2, together with the inward bending of TM1, TM4, TM5 and TM6 of UCP1, resulting in a more compact structure of UCP1. The binding site of ATP overlaps with that of DNP, suggesting that ATP competitively blocks the functional engagement of DNP, resulting in the inhibition of the proton-conducting activity of UCP1.
Author	Kang, Yunlu Chen, Lei
Author_xml	– sequence: 1 givenname: Yunlu orcidid: 0000-0001-8179-4487 surname: Kang fullname: Kang, Yunlu organization: State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine – sequence: 2 givenname: Lei orcidid: 0000-0002-7619-8311 surname: Chen fullname: Chen, Lei email: chenlei2016@pku.edu.cn organization: State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking-Tsinghua Center for Life Sciences, Peking University, Academy for Advanced Interdisciplinary Studies, Peking University, National Biomedical Imaging Center, Peking University
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Cites_doi	10.1016/j.biochi.2016.10.013 10.1074/jbc.272.40.24759 10.1152/physrev.1984.64.1.1 10.1016/j.biochi.2016.12.016 10.1016/j.cmet.2018.11.002 10.1038/nmeth.4169 10.1038/s41586-021-03819-2 10.1146/annurev.biophys.30.1.23 10.1074/jbc.273.38.24368 10.1038/s41467-019-12301-7 10.1016/j.biochi.2016.10.018 10.1016/j.cell.2012.09.010 10.1038/s41467-022-31366-5 10.1093/bioinformatics/bty386 10.7554/eLife.42166 10.1016/j.crvi.2005.10.010 10.1016/j.molmet.2017.12.010 10.1002/pro.3943 10.1021/ci200227u 10.1016/S0006-3495(93)81293-1 10.3390/biom11081178 10.1073/pnas.2115001118 10.1016/j.molmet.2022.101526 10.1107/S2059798318006551 10.1038/nmeth.4079 10.1016/j.cell.2016.05.022 10.1016/j.jsb.2015.11.003 10.1038/s41596-020-0304-x 10.1038/nmeth.4193 10.1021/bi962178x 10.1021/acs.jpcb.6b08339 10.1152/physiol.00046.2010 10.1016/j.febslet.2005.09.061 10.1038/s41586-019-1400-3 10.1093/nar/gku316 10.1038/nprot.2014.173 10.1016/j.cell.2020.11.043 10.3389/fendo.2020.00118 10.1073/pnas.0509994103 10.1038/s41592-020-00990-8 10.1038/s42003-021-01891-y 10.1186/s10020-020-00180-4 10.1016/j.bbabio.2006.05.005 10.1152/physiol.00009.2020 10.1016/j.biochi.2016.10.012 10.1002/jcc.20084 10.1016/j.cell.2018.11.025 10.1038/s41592-019-0575-8 10.1016/j.ultramic.2013.06.004 10.3109/09687688.2012.745175 10.1111/j.1432-1033.1969.tb00759.x 10.1002/j.1460-2075.1985.tb03941.x 10.1016/j.biochi.2016.09.003 10.1016/j.cell.2016.12.028 10.1146/annurev-biochem-072820-020508 10.7554/eLife.34317 10.1021/bi970513r 10.1073/pnas.1503833112 10.1038/nature02056 10.1093/bioinformatics/btm404 10.1038/s41586-022-04747-5 10.1515/bchm2.1969.350.2.1121 10.1107/S0907444910007493
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References	Jin (CR43) 2021; 4 Rafael, Ludolph, Hohorst (CR10) 1969; 350 Echtay, Bienengraeber, Klingenberg (CR30) 1997; 36 Bertholet, Kirichok (CR35) 2017; 134 Bertholet (CR4) 2022; 606 Pravednikova (CR13) 2020; 26 Mavridou (CR24) 2022; 13 Nury (CR26) 2005; 579 Kunji, King, Ruprecht, Thangaratnarajah (CR15) 2020; 35 Modriansky, Murdza-Inglis, Patel, Freeman, Garlid (CR33) 1997; 272 Smart, Goodfellow, Wallace (CR61) 1993; 65 Jurcik (CR60) 2018; 34 Afonine (CR56) 2018; 74 Chouchani, Kazak, Spiegelman (CR2) 2019; 29 Aquila, Link, Klingenberg (CR14) 1985; 4 Lee, Willers, Kunji, Crichton (CR20) 2015; 112 Wu, Rapoport (CR23) 2021; 118 Crichton, Lee, Kunji (CR17) 2017; 134 Dlaskova, Spacek, Skobisova, Santorova, Jezek (CR32) 2006; 1757 van Keulen (CR36) 2017; 121 Robert, Gouet (CR59) 2014; 42 Cavalieri (CR28) 2022; 62 Zhang (CR46) 2016; 193 Zimmermann (CR22) 2018; 7 Zimmermann (CR21) 2020; 15 Götzke (CR42) 2019; 10 Nicholls (CR7) 2017; 134 Pettersen (CR54) 2004; 25 Larkin (CR58) 2007; 23 Gong (CR51) 2016; 165 Bast-Habersbrunner, Fromme (CR19) 2020; 11 Chen (CR63) 2013; 135 Pettersen (CR57) 2021; 30 Bepler (CR50) 2019; 16 Zivanov (CR52) 2018; 7 Zuna (CR5) 2021; 11 Nicholls, Locke (CR11) 1984; 64 Ruprecht, Kunji (CR16) 2021; 90 Schultz, Chan (CR6) 2001; 30 Bertholet (CR37) 2019; 571 Divakaruni, Brand (CR1) 2011; 26 Wang (CR49) 2021; 184 Emsley, Lohkamp, Scott, Cowtan (CR55) 2010; 66 Jumper (CR53) 2021; 596 Mifsud (CR39) 2013; 30 Li (CR40) 2017; 168 Laskowski, Swindells (CR62) 2011; 51 Nasr (CR44) 2017; 14 Punjani, Rubinstein, Fleet, Brubaker (CR47) 2017; 14 Zheng (CR45) 2017; 14 Ruprecht (CR27) 2019; 176 Robinson, Kunji (CR38) 2006; 103 Punjani, Zhang, Fleet (CR48) 2020; 17 Hittelman, Lindberg, Cannon (CR9) 1969; 11 Pebay-Peyroula (CR25) 2003; 426 Goehring (CR41) 2014; 9 Fedorenko, Lishko, Kirichok (CR34) 2012; 151 Winkler, Wachter, Klingenberg (CR29) 1997; 36 Ricquier (CR12) 2006; 329 Ricquier (CR8) 2017; 134 Klingenberg (CR3) 2017; 134 Echtay, Bienengraeber, Winkler, Klingenberg (CR31) 1998; 273 Fromme (CR18) 2018; 8 EF Pettersen (6332_CR57) 2021; 30 SQ Zheng (6332_CR45) 2017; 14 PV Afonine (6332_CR56) 2018; 74 P Emsley (6332_CR55) 2010; 66 I Zimmermann (6332_CR21) 2020; 15 E Pebay-Peyroula (6332_CR25) 2003; 426 JJ Ruprecht (6332_CR27) 2019; 176 M Klingenberg (6332_CR3) 2017; 134 D Ricquier (6332_CR12) 2006; 329 AM Bertholet (6332_CR35) 2017; 134 AM Bertholet (6332_CR37) 2019; 571 A Punjani (6332_CR48) 2020; 17 ET Chouchani (6332_CR2) 2019; 29 F Jin (6332_CR43) 2021; 4 N Li (6332_CR40) 2017; 168 X Robert (6332_CR59) 2014; 42 RA Laskowski (6332_CR62) 2011; 51 A Punjani (6332_CR47) 2017; 14 X Wu (6332_CR23) 2021; 118 DG Nicholls (6332_CR11) 1984; 64 J Mifsud (6332_CR39) 2013; 30 H Götzke (6332_CR42) 2019; 10 A Goehring (6332_CR41) 2014; 9 E Winkler (6332_CR29) 1997; 36 T Fromme (6332_CR18) 2018; 8 J Jumper (6332_CR53) 2021; 596 H Nury (6332_CR26) 2005; 579 M Modriansky (6332_CR33) 1997; 272 AM Bertholet (6332_CR4) 2022; 606 ERS Kunji (6332_CR15) 2020; 35 A Dlaskova (6332_CR32) 2006; 1757 X Gong (6332_CR51) 2016; 165 A Fedorenko (6332_CR34) 2012; 151 KJ Hittelman (6332_CR9) 1969; 11 KS Echtay (6332_CR30) 1997; 36 N Wang (6332_CR49) 2021; 184 PG Crichton (6332_CR17) 2017; 134 OS Smart (6332_CR61) 1993; 65 Y Lee (6332_CR20) 2015; 112 AE Pravednikova (6332_CR13) 2020; 26 DG Nicholls (6332_CR7) 2017; 134 T Bepler (6332_CR50) 2019; 16 AJ Robinson (6332_CR38) 2006; 103 S Chen (6332_CR63) 2013; 135 H Aquila (6332_CR14) 1985; 4 KS Echtay (6332_CR31) 1998; 273 A Bast-Habersbrunner (6332_CR19) 2020; 11 J Rafael (6332_CR10) 1969; 350 K Zuna (6332_CR5) 2021; 11 V Mavridou (6332_CR24) 2022; 13 D Ricquier (6332_CR8) 2017; 134 AS Divakaruni (6332_CR1) 2011; 26 MA Larkin (6332_CR58) 2007; 23 SC van Keulen (6332_CR36) 2017; 121 J Zivanov (6332_CR52) 2018; 7 JJ Ruprecht (6332_CR16) 2021; 90 BE Schultz (6332_CR6) 2001; 30 R Cavalieri (6332_CR28) 2022; 62 ML Nasr (6332_CR44) 2017; 14 EF Pettersen (6332_CR54) 2004; 25 I Zimmermann (6332_CR22) 2018; 7 A Jurcik (6332_CR60) 2018; 34 K Zhang (6332_CR46) 2016; 193
References_xml	– volume: 134 start-page: 28 year: 2017 end-page: 34 ident: CR35 article-title: UCP1: a transporter for H and fatty acid anions publication-title: Biochimie doi: 10.1016/j.biochi.2016.10.013 – volume: 272 start-page: 24759 year: 1997 end-page: 24762 ident: CR33 article-title: Identification by site-directed mutagenesis of three arginines in uncoupling protein that are essential for nucleotide binding and inhibition publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.40.24759 – volume: 64 start-page: 1 year: 1984 end-page: 64 ident: CR11 article-title: Thermogenic mechanisms in brown fat publication-title: Physiol. Rev. doi: 10.1152/physrev.1984.64.1.1 – volume: 134 start-page: 35 year: 2017 end-page: 50 ident: CR17 article-title: The molecular features of uncoupling protein 1 support a conventional mitochondrial carrier-like mechanism publication-title: Biochimie doi: 10.1016/j.biochi.2016.12.016 – volume: 29 start-page: 27 year: 2019 end-page: 37 ident: CR2 article-title: New advances in adaptive thermogenesis: UCP1 and beyond publication-title: Cell Metab. doi: 10.1016/j.cmet.2018.11.002 – volume: 14 start-page: 290 year: 2017 end-page: 296 ident: CR47 article-title: cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination publication-title: Nat. Methods doi: 10.1038/nmeth.4169 – volume: 596 start-page: 583 year: 2021 end-page: 589 ident: CR53 article-title: Highly accurate protein structure prediction with AlphaFold publication-title: Nature doi: 10.1038/s41586-021-03819-2 – volume: 30 start-page: 23 year: 2001 end-page: 65 ident: CR6 article-title: Structures and proton-pumping strategies of mitochondrial respiratory enzymes publication-title: Annu. Rev. Biophys. Biomol. Struct. doi: 10.1146/annurev.biophys.30.1.23 – volume: 273 start-page: 24368 year: 1998 end-page: 24374 ident: CR31 article-title: In the uncoupling protein (UCP-1) His-214 is involved in the regulation of purine nucleoside triphosphate but not diphosphate binding publication-title: J. Biol. Chem. doi: 10.1074/jbc.273.38.24368 – volume: 10 year: 2019 ident: CR42 article-title: The ALFA-tag is a highly versatile tool for nanobody-based bioscience applications publication-title: Nat. Commun. doi: 10.1038/s41467-019-12301-7 – volume: 134 start-page: 3 year: 2017 end-page: 8 ident: CR8 article-title: UCP1, the mitochondrial uncoupling protein of brown adipocyte: a personal contribution and a historical perspective publication-title: Biochimie doi: 10.1016/j.biochi.2016.10.018 – volume: 151 start-page: 400 year: 2012 end-page: 413 ident: CR34 article-title: Mechanism of fatty-acid-dependent UCP1 uncoupling in brown fat mitochondria publication-title: Cell doi: 10.1016/j.cell.2012.09.010 – volume: 13 year: 2022 ident: CR24 article-title: Substrate binding in the mitochondrial ADP/ATP carrier is a step-wise process guiding the structural changes in the transport cycle publication-title: Nat. Commun. doi: 10.1038/s41467-022-31366-5 – volume: 34 start-page: 3586 year: 2018 end-page: 3588 ident: CR60 article-title: CAVER Analyst 2.0: analysis and visualization of channels and tunnels in protein structures and molecular dynamics trajectories publication-title: Bioinformatics doi: 10.1093/bioinformatics/bty386 – volume: 7 start-page: e42166 year: 2018 ident: CR52 article-title: New tools for automated high-resolution cryo-EM structure determination in RELION-3 publication-title: eLife doi: 10.7554/eLife.42166 – volume: 329 start-page: 578 year: 2006 end-page: 586; discussion 653–655 ident: CR12 article-title: Fundamental mechanisms of thermogenesis publication-title: C. R. Biol. doi: 10.1016/j.crvi.2005.10.010 – volume: 8 start-page: 77 year: 2018 end-page: 85 ident: CR18 article-title: Degradation of brown adipocyte purine nucleotides regulates uncoupling protein 1 activity publication-title: Mol. Metab. doi: 10.1016/j.molmet.2017.12.010 – volume: 30 start-page: 70 year: 2021 end-page: 82 ident: CR57 article-title: UCSF ChimeraX: structure visualization for researchers, educators, and developers publication-title: Protein Sci. doi: 10.1002/pro.3943 – volume: 51 start-page: 2778 year: 2011 end-page: 2786 ident: CR62 article-title: LigPlot+: multiple ligand–protein interaction diagrams for drug discovery publication-title: J. Chem. Inf. Model. doi: 10.1021/ci200227u – volume: 65 start-page: 2455 year: 1993 end-page: 2460 ident: CR61 article-title: The pore dimensions of gramicidin A publication-title: Biophys. J. doi: 10.1016/S0006-3495(93)81293-1 – volume: 11 start-page: 1178 year: 2021 ident: CR5 article-title: Mitochondrial uncoupling proteins (UCP1–UCP3) and adenine nucleotide translocase (ANT1) enhance the protonophoric action of 2,4-dinitrophenol in mitochondria and planar bilayer membranes publication-title: Biomolecules doi: 10.3390/biom11081178 – volume: 118 start-page: e2115001118 year: 2021 ident: CR23 article-title: Cryo-EM structure determination of small proteins by nanobody-binding scaffolds (legobodies) publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.2115001118 – volume: 62 start-page: 101526 year: 2022 ident: CR28 article-title: Activating ligands of uncoupling protein 1 identified by rapid membrane protein thermostability shift analysis publication-title: Mol. Metab. doi: 10.1016/j.molmet.2022.101526 – volume: 74 start-page: 531 year: 2018 end-page: 544 ident: CR56 article-title: Real-space refinement in PHENIX for cryo-EM and crystallography publication-title: Acta Crystallogr. D Struct. Biol. doi: 10.1107/S2059798318006551 – volume: 14 start-page: 49 year: 2017 end-page: 52 ident: CR44 article-title: Covalently circularized nanodiscs for studying membrane proteins and viral entry publication-title: Nat. Methods doi: 10.1038/nmeth.4079 – volume: 165 start-page: 1467 year: 2016 end-page: 1478 ident: CR51 article-title: Structural insights into the Niemann–Pick C1 (NPC1)-mediated cholesterol transfer and Ebola infection publication-title: Cell doi: 10.1016/j.cell.2016.05.022 – volume: 193 start-page: 1 year: 2016 end-page: 12 ident: CR46 article-title: Gctf: real-time CTF determination and correction publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2015.11.003 – volume: 15 start-page: 1707 year: 2020 end-page: 1741 ident: CR21 article-title: Generation of synthetic nanobodies against delicate proteins publication-title: Nat. Protoc. doi: 10.1038/s41596-020-0304-x – volume: 14 start-page: 331 year: 2017 end-page: 332 ident: CR45 article-title: MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy publication-title: Nat. Methods doi: 10.1038/nmeth.4193 – volume: 36 start-page: 148 year: 1997 end-page: 155 ident: CR29 article-title: Identification of the pH sensor for nucleotide binding in the uncoupling protein from brown adipose tissue publication-title: Biochemistry doi: 10.1021/bi962178x – volume: 121 start-page: 3340 year: 2017 end-page: 3351 ident: CR36 article-title: Does proton conduction in the voltage-gated H channel hHv1 involve Grotthuss-like hopping via acidic residues? publication-title: J. Phys. Chem. B doi: 10.1021/acs.jpcb.6b08339 – volume: 26 start-page: 192 year: 2011 end-page: 205 ident: CR1 article-title: The regulation and physiology of mitochondrial proton leak publication-title: Physiology doi: 10.1152/physiol.00046.2010 – volume: 579 start-page: 6031 year: 2005 end-page: 6036 ident: CR26 article-title: Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers publication-title: FEBS Lett. doi: 10.1016/j.febslet.2005.09.061 – volume: 571 start-page: 515 year: 2019 end-page: 520 ident: CR37 article-title: H transport is an integral function of the mitochondrial ADP/ATP carrier publication-title: Nature doi: 10.1038/s41586-019-1400-3 – volume: 42 start-page: W320 year: 2014 end-page: W324 ident: CR59 article-title: Deciphering key features in protein structures with the new ENDscript server publication-title: Nucleic Acids Res. doi: 10.1093/nar/gku316 – volume: 9 start-page: 2574 year: 2014 end-page: 2585 ident: CR41 article-title: Screening and large-scale expression of membrane proteins in mammalian cells for structural studies publication-title: Nat. Protoc. doi: 10.1038/nprot.2014.173 – volume: 184 start-page: 370 year: 2021 end-page: 383.e13 ident: CR49 article-title: Structural basis of human monocarboxylate transporter 1 inhibition by anti-cancer drug candidates publication-title: Cell doi: 10.1016/j.cell.2020.11.043 – volume: 11 start-page: 118 year: 2020 ident: CR19 article-title: Purine nucleotides in the regulation of brown adipose tissue activity publication-title: Front. Endocrinol. doi: 10.3389/fendo.2020.00118 – volume: 103 start-page: 2617 year: 2006 end-page: 2622 ident: CR38 article-title: Mitochondrial carriers in the cytoplasmic state have a common substrate binding site publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.0509994103 – volume: 17 start-page: 1214 year: 2020 end-page: 1221 ident: CR48 article-title: Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction publication-title: Nat. Methods doi: 10.1038/s41592-020-00990-8 – volume: 4 start-page: 366 year: 2021 ident: CR43 article-title: Fluorescence-detection size-exclusion chromatography utilizing nanobody technology for expression screening of membrane proteins publication-title: Commun. Biol. doi: 10.1038/s42003-021-01891-y – volume: 26 start-page: 51 year: 2020 ident: CR13 article-title: Association of uncoupling protein (Ucp) gene polymorphisms with cardiometabolic diseases publication-title: Mol. Med. doi: 10.1186/s10020-020-00180-4 – volume: 1757 start-page: 467 year: 2006 end-page: 473 ident: CR32 article-title: Certain aspects of uncoupling due to mitochondrial uncoupling proteins in vitro and in vivo publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbabio.2006.05.005 – volume: 35 start-page: 302 year: 2020 end-page: 327 ident: CR15 article-title: The SLC25 carrier family: important transport proteins in mitochondrial physiology and pathology publication-title: Physiology doi: 10.1152/physiol.00009.2020 – volume: 134 start-page: 19 year: 2017 end-page: 27 ident: CR3 article-title: UCP1—a sophisticated energy valve publication-title: Biochimie doi: 10.1016/j.biochi.2016.10.012 – volume: 25 start-page: 1605 year: 2004 end-page: 1612 ident: CR54 article-title: UCSF Chimera—a visualization system for exploratory research and analysis publication-title: J. Comput. Chem. doi: 10.1002/jcc.20084 – volume: 176 start-page: 435 year: 2019 end-page: 447.e15 ident: CR27 article-title: The molecular mechanism of transport by the mitochondrial ADP/ATP carrier publication-title: Cell doi: 10.1016/j.cell.2018.11.025 – volume: 16 start-page: 1153 year: 2019 end-page: 1160 ident: CR50 article-title: Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs publication-title: Nat. Methods doi: 10.1038/s41592-019-0575-8 – volume: 135 start-page: 24 year: 2013 end-page: 35 ident: CR63 article-title: High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy publication-title: Ultramicroscopy doi: 10.1016/j.ultramic.2013.06.004 – volume: 30 start-page: 160 year: 2013 end-page: 168 ident: CR39 article-title: The substrate specificity of the human ADP/ATP carrier AAC1 publication-title: Mol. Membr. Biol. doi: 10.3109/09687688.2012.745175 – volume: 11 start-page: 183 year: 1969 end-page: 192 ident: CR9 article-title: Oxidative phosphorylation and compartmentation of fatty acid metabolism in brown fat mitochondria publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1969.tb00759.x – volume: 4 start-page: 2369 year: 1985 end-page: 2376 ident: CR14 article-title: The uncoupling protein from brown fat mitochondria is related to the mitochondrial ADP/ATP carrier. Analysis of sequence homologies and of folding of the protein in the membrane publication-title: EMBO J. doi: 10.1002/j.1460-2075.1985.tb03941.x – volume: 134 start-page: 9 year: 2017 end-page: 18 ident: CR7 article-title: The hunt for the molecular mechanism of brown fat thermogenesis publication-title: Biochimie doi: 10.1016/j.biochi.2016.09.003 – volume: 168 start-page: 101 year: 2017 end-page: 110.e10 ident: CR40 article-title: Structure of a pancreatic ATP-sensitive potassium channel publication-title: Cell doi: 10.1016/j.cell.2016.12.028 – volume: 90 start-page: 535 year: 2021 end-page: 558 ident: CR16 article-title: Structural mechanism of transport of mitochondrial carriers publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev-biochem-072820-020508 – volume: 7 start-page: e34317 year: 2018 ident: CR22 article-title: Synthetic single domain antibodies for the conformational trapping of membrane proteins publication-title: eLife doi: 10.7554/eLife.34317 – volume: 36 start-page: 8253 year: 1997 end-page: 8260 ident: CR30 article-title: Mutagenesis of the uncoupling protein of brown adipose tissue. Neutralization of E190 largely abolishes pH control of nucleotide binding publication-title: Biochemistry doi: 10.1021/bi970513r – volume: 112 start-page: 6973 year: 2015 end-page: 6978 ident: CR20 article-title: Uncoupling protein 1 binds one nucleotide per monomer and is stabilized by tightly bound cardiolipin publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1503833112 – volume: 426 start-page: 39 year: 2003 end-page: 44 ident: CR25 article-title: Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside publication-title: Nature doi: 10.1038/nature02056 – volume: 23 start-page: 2947 year: 2007 end-page: 2948 ident: CR58 article-title: Clustal W and Clustal X version 2.0 publication-title: Bioinformatics doi: 10.1093/bioinformatics/btm404 – volume: 606 start-page: 180 year: 2022 end-page: 187 ident: CR4 article-title: Mitochondrial uncouplers induce proton leak by activating AAC and UCP1 publication-title: Nature doi: 10.1038/s41586-022-04747-5 – volume: 350 start-page: 1121 year: 1969 end-page: 1131 ident: CR10 article-title: [Mitochondria from brown adipose tissue: uncoupling of respiratory chain phosphorylation by long fatty acids and recoupling by guanosine triphosphate] publication-title: Hoppe Seylers Z Physiol. Chem. doi: 10.1515/bchm2.1969.350.2.1121 – volume: 66 start-page: 486 year: 2010 end-page: 501 ident: CR55 article-title: Features and development of Coot publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S0907444910007493 – volume: 14 start-page: 49 year: 2017 ident: 6332_CR44 publication-title: Nat. Methods doi: 10.1038/nmeth.4079 – volume: 134 start-page: 9 year: 2017 ident: 6332_CR7 publication-title: Biochimie doi: 10.1016/j.biochi.2016.09.003 – volume: 10 year: 2019 ident: 6332_CR42 publication-title: Nat. Commun. doi: 10.1038/s41467-019-12301-7 – volume: 134 start-page: 28 year: 2017 ident: 6332_CR35 publication-title: Biochimie doi: 10.1016/j.biochi.2016.10.013 – volume: 62 start-page: 101526 year: 2022 ident: 6332_CR28 publication-title: Mol. Metab. doi: 10.1016/j.molmet.2022.101526 – volume: 29 start-page: 27 year: 2019 ident: 6332_CR2 publication-title: Cell Metab. doi: 10.1016/j.cmet.2018.11.002 – volume: 350 start-page: 1121 year: 1969 ident: 6332_CR10 publication-title: Hoppe Seylers Z Physiol. Chem. doi: 10.1515/bchm2.1969.350.2.1121 – volume: 51 start-page: 2778 year: 2011 ident: 6332_CR62 publication-title: J. Chem. Inf. Model. doi: 10.1021/ci200227u – volume: 23 start-page: 2947 year: 2007 ident: 6332_CR58 publication-title: Bioinformatics doi: 10.1093/bioinformatics/btm404 – volume: 13 year: 2022 ident: 6332_CR24 publication-title: Nat. Commun. doi: 10.1038/s41467-022-31366-5 – volume: 1757 start-page: 467 year: 2006 ident: 6332_CR32 publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbabio.2006.05.005 – volume: 168 start-page: 101 year: 2017 ident: 6332_CR40 publication-title: Cell doi: 10.1016/j.cell.2016.12.028 – volume: 273 start-page: 24368 year: 1998 ident: 6332_CR31 publication-title: J. Biol. Chem. doi: 10.1074/jbc.273.38.24368 – volume: 30 start-page: 160 year: 2013 ident: 6332_CR39 publication-title: Mol. Membr. Biol. doi: 10.3109/09687688.2012.745175 – volume: 30 start-page: 70 year: 2021 ident: 6332_CR57 publication-title: Protein Sci. doi: 10.1002/pro.3943 – volume: 14 start-page: 331 year: 2017 ident: 6332_CR45 publication-title: Nat. Methods doi: 10.1038/nmeth.4193 – volume: 64 start-page: 1 year: 1984 ident: 6332_CR11 publication-title: Physiol. Rev. doi: 10.1152/physrev.1984.64.1.1 – volume: 11 start-page: 118 year: 2020 ident: 6332_CR19 publication-title: Front. Endocrinol. doi: 10.3389/fendo.2020.00118 – volume: 176 start-page: 435 year: 2019 ident: 6332_CR27 publication-title: Cell doi: 10.1016/j.cell.2018.11.025 – volume: 134 start-page: 19 year: 2017 ident: 6332_CR3 publication-title: Biochimie doi: 10.1016/j.biochi.2016.10.012 – volume: 65 start-page: 2455 year: 1993 ident: 6332_CR61 publication-title: Biophys. J. doi: 10.1016/S0006-3495(93)81293-1 – volume: 9 start-page: 2574 year: 2014 ident: 6332_CR41 publication-title: Nat. Protoc. doi: 10.1038/nprot.2014.173 – volume: 17 start-page: 1214 year: 2020 ident: 6332_CR48 publication-title: Nat. Methods doi: 10.1038/s41592-020-00990-8 – volume: 606 start-page: 180 year: 2022 ident: 6332_CR4 publication-title: Nature doi: 10.1038/s41586-022-04747-5 – volume: 90 start-page: 535 year: 2021 ident: 6332_CR16 publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev-biochem-072820-020508 – volume: 15 start-page: 1707 year: 2020 ident: 6332_CR21 publication-title: Nat. Protoc. doi: 10.1038/s41596-020-0304-x – volume: 4 start-page: 2369 year: 1985 ident: 6332_CR14 publication-title: EMBO J. doi: 10.1002/j.1460-2075.1985.tb03941.x – volume: 571 start-page: 515 year: 2019 ident: 6332_CR37 publication-title: Nature doi: 10.1038/s41586-019-1400-3 – volume: 42 start-page: W320 year: 2014 ident: 6332_CR59 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gku316 – volume: 30 start-page: 23 year: 2001 ident: 6332_CR6 publication-title: Annu. Rev. Biophys. Biomol. Struct. doi: 10.1146/annurev.biophys.30.1.23 – volume: 579 start-page: 6031 year: 2005 ident: 6332_CR26 publication-title: FEBS Lett. doi: 10.1016/j.febslet.2005.09.061 – volume: 193 start-page: 1 year: 2016 ident: 6332_CR46 publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2015.11.003 – volume: 184 start-page: 370 year: 2021 ident: 6332_CR49 publication-title: Cell doi: 10.1016/j.cell.2020.11.043 – volume: 26 start-page: 51 year: 2020 ident: 6332_CR13 publication-title: Mol. Med. doi: 10.1186/s10020-020-00180-4 – volume: 134 start-page: 3 year: 2017 ident: 6332_CR8 publication-title: Biochimie doi: 10.1016/j.biochi.2016.10.018 – volume: 16 start-page: 1153 year: 2019 ident: 6332_CR50 publication-title: Nat. Methods doi: 10.1038/s41592-019-0575-8 – volume: 4 start-page: 366 year: 2021 ident: 6332_CR43 publication-title: Commun. Biol. doi: 10.1038/s42003-021-01891-y – volume: 14 start-page: 290 year: 2017 ident: 6332_CR47 publication-title: Nat. Methods doi: 10.1038/nmeth.4169 – volume: 74 start-page: 531 year: 2018 ident: 6332_CR56 publication-title: Acta Crystallogr. D Struct. Biol. doi: 10.1107/S2059798318006551 – volume: 121 start-page: 3340 year: 2017 ident: 6332_CR36 publication-title: J. Phys. Chem. B doi: 10.1021/acs.jpcb.6b08339 – volume: 135 start-page: 24 year: 2013 ident: 6332_CR63 publication-title: Ultramicroscopy doi: 10.1016/j.ultramic.2013.06.004 – volume: 35 start-page: 302 year: 2020 ident: 6332_CR15 publication-title: Physiology doi: 10.1152/physiol.00009.2020 – volume: 7 start-page: e34317 year: 2018 ident: 6332_CR22 publication-title: eLife doi: 10.7554/eLife.34317 – volume: 165 start-page: 1467 year: 2016 ident: 6332_CR51 publication-title: Cell doi: 10.1016/j.cell.2016.05.022 – volume: 134 start-page: 35 year: 2017 ident: 6332_CR17 publication-title: Biochimie doi: 10.1016/j.biochi.2016.12.016 – volume: 25 start-page: 1605 year: 2004 ident: 6332_CR54 publication-title: J. Comput. Chem. doi: 10.1002/jcc.20084 – volume: 272 start-page: 24759 year: 1997 ident: 6332_CR33 publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.40.24759 – volume: 426 start-page: 39 year: 2003 ident: 6332_CR25 publication-title: Nature doi: 10.1038/nature02056 – volume: 11 start-page: 183 year: 1969 ident: 6332_CR9 publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1969.tb00759.x – volume: 8 start-page: 77 year: 2018 ident: 6332_CR18 publication-title: Mol. Metab. doi: 10.1016/j.molmet.2017.12.010 – volume: 7 start-page: e42166 year: 2018 ident: 6332_CR52 publication-title: eLife doi: 10.7554/eLife.42166 – volume: 34 start-page: 3586 year: 2018 ident: 6332_CR60 publication-title: Bioinformatics doi: 10.1093/bioinformatics/bty386 – volume: 118 start-page: e2115001118 year: 2021 ident: 6332_CR23 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.2115001118 – volume: 112 start-page: 6973 year: 2015 ident: 6332_CR20 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1503833112 – volume: 329 start-page: 578 year: 2006 ident: 6332_CR12 publication-title: C. R. Biol. doi: 10.1016/j.crvi.2005.10.010 – volume: 151 start-page: 400 year: 2012 ident: 6332_CR34 publication-title: Cell doi: 10.1016/j.cell.2012.09.010 – volume: 11 start-page: 1178 year: 2021 ident: 6332_CR5 publication-title: Biomolecules doi: 10.3390/biom11081178 – volume: 596 start-page: 583 year: 2021 ident: 6332_CR53 publication-title: Nature doi: 10.1038/s41586-021-03819-2 – volume: 66 start-page: 486 year: 2010 ident: 6332_CR55 publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S0907444910007493 – volume: 26 start-page: 192 year: 2011 ident: 6332_CR1 publication-title: Physiology doi: 10.1152/physiol.00046.2010 – volume: 36 start-page: 148 year: 1997 ident: 6332_CR29 publication-title: Biochemistry doi: 10.1021/bi962178x – volume: 36 start-page: 8253 year: 1997 ident: 6332_CR30 publication-title: Biochemistry doi: 10.1021/bi970513r – volume: 103 start-page: 2617 year: 2006 ident: 6332_CR38 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.0509994103
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Snippet	Uncoupling protein 1 (UCP1) conducts protons through the inner mitochondrial membrane to uncouple mitochondrial respiration from ATP production, thereby...
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SubjectTerms	101/28 2,4-Dinitrophenol 2,4-Dinitrophenol - chemistry 2,4-Dinitrophenol - metabolism 631/45/612/1237 631/535/1258/1259 82/80 82/83 Adenosine triphosphate Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism ATP Binding sites Cell Membrane - metabolism Cytosol - metabolism Electrochemistry Electron transport Fatty acids Fatty Acids - metabolism Humanities and Social Sciences Humans Lipids multidisciplinary Nucleotides Permeability Protein Conformation Proteins Protons Respiration Science Science (multidisciplinary) Uncoupling protein 1 Uncoupling Protein 1 - chemistry Uncoupling Protein 1 - metabolism
Title	Structural basis for the binding of DNP and purine nucleotides onto UCP1
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