Molecular basis for interactions between an acyl carrier protein and a ketosynthase
Fatty acid synthases are dynamic ensembles of enzymes that can biosynthesize long hydrocarbon chains efficiently. Here we visualize the interaction between the Escherichia coli acyl carrier protein (AcpP) and β-ketoacyl-ACP-synthase I (FabB) using X-ray crystallography, NMR, and molecular dynamics s...
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| Veröffentlicht in: | Nature chemical biology Jg. 15; H. 7; S. 669 - 671 |
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| Hauptverfasser: | , , , , , , , , , |
| Format: | Journal Article |
| Sprache: | Englisch |
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01.07.2019
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| ISSN: | 1552-4450, 1552-4469, 1552-4469 |
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| Abstract | Fatty acid synthases are dynamic ensembles of enzymes that can biosynthesize long hydrocarbon chains efficiently. Here we visualize the interaction between the
Escherichia coli
acyl carrier protein (AcpP) and β-ketoacyl-ACP-synthase I (FabB) using X-ray crystallography, NMR, and molecular dynamics simulations. We leveraged this structural information to alter lipid profiles in vivo and provide a molecular basis for how protein–protein interactions can regulate the fatty acid profile in
E. coli
.
A combination of crosslinking, X-ray crystallography, NMR, and mutagenesis provide a detailed visualization of the interactions between an acyl carrier protein and β-ketoacyl-ACP-synthase I in the
Escherchia coli
fatty acid synthase complex. |
|---|---|
| AbstractList | Fatty acid synthases are dynamic ensembles of enzymes that can biosynthesize long hydrocarbon chains efficiently. Here we visualize the interaction between the Escherichia coli acyl carrier protein (AcpP) and β-ketoacyl-ACP-synthase I (FabB) using X-ray crystallography, NMR, and molecular dynamics simulations. We leveraged this structural information to alter lipid profiles in vivo and provide a molecular basis for how protein-protein interactions can regulate the fatty acid profile in E. coli.Fatty acid synthases are dynamic ensembles of enzymes that can biosynthesize long hydrocarbon chains efficiently. Here we visualize the interaction between the Escherichia coli acyl carrier protein (AcpP) and β-ketoacyl-ACP-synthase I (FabB) using X-ray crystallography, NMR, and molecular dynamics simulations. We leveraged this structural information to alter lipid profiles in vivo and provide a molecular basis for how protein-protein interactions can regulate the fatty acid profile in E. coli. Fatty acid synthases are dynamic ensembles of enzymes that can efficiently biosynthesize long hydrocarbon chains. Here we visualize the interaction between the Escherichia coli acyl carrier protein (AcpP) and β-ketoacyl-ACP-synthase I (FabB) using X-ray crystallography, NMR, and MD simulations. We leveraged this structural information to alter lipid profiles in vivo and provide a molecular basis for how protein-protein interactions can regulate the fatty acid profile in E. coli. Fatty acid synthases are dynamic ensembles of enzymes that can biosynthesize long hydrocarbon chains efficiently. Here we visualize the interaction between the Escherichia coli acyl carrier protein (AcpP) and β-ketoacyl-ACP-synthase I (FabB) using X-ray crystallography, NMR, and molecular dynamics simulations. We leveraged this structural information to alter lipid profiles in vivo and provide a molecular basis for how protein-protein interactions can regulate the fatty acid profile in E. coli. Fatty acid synthases are dynamic ensembles of enzymes that can biosynthesize long hydrocarbon chains efficiently. Here we visualize the interaction between the Escherichia coli acyl carrier protein (AcpP) and β-ketoacyl-ACP-synthase I (FabB) using X-ray crystallography, NMR, and molecular dynamics simulations. We leveraged this structural information to alter lipid profiles in vivo and provide a molecular basis for how protein–protein interactions can regulate the fatty acid profile in E. coli . A combination of crosslinking, X-ray crystallography, NMR, and mutagenesis provide a detailed visualization of the interactions between an acyl carrier protein and β-ketoacyl-ACP-synthase I in the Escherchia coli fatty acid synthase complex. |
| Author | Jackson, David R. Beld, Joris Milligan, Jacob C. Tsai, Shiou-Chuan Lee, D. John Luo, Ray Burkart, Michael D. Schaub, Andrew J. Barajas, Jesus F. Hale, Joseph J. |
| AuthorAffiliation | 2 Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA 4 Department of Pharmaceutical Sciences, University of California, Irvine, CA, USA 5 These authors contributed equally to this work 3 Department of Chemistry, University of California, Irvine, CA, USA 1 Department of Molecular Biology and Biochemistry, University of California, Irvine, CA, USA |
| AuthorAffiliation_xml | – name: 5 These authors contributed equally to this work – name: 3 Department of Chemistry, University of California, Irvine, CA, USA – name: 1 Department of Molecular Biology and Biochemistry, University of California, Irvine, CA, USA – name: 4 Department of Pharmaceutical Sciences, University of California, Irvine, CA, USA – name: 2 Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA |
| Author_xml | – sequence: 1 givenname: Jacob C. surname: Milligan fullname: Milligan, Jacob C. organization: Department of Molecular Biology and Biochemistry, University of California, Irvine – sequence: 2 givenname: D. John surname: Lee fullname: Lee, D. John organization: Department of Chemistry and Biochemistry, University of California, San Diego – sequence: 3 givenname: David R. surname: Jackson fullname: Jackson, David R. organization: Department of Chemistry, University of California, Irvine – sequence: 4 givenname: Andrew J. orcidid: 0000-0001-7770-7045 surname: Schaub fullname: Schaub, Andrew J. organization: Department of Chemistry, University of California, Irvine – sequence: 5 givenname: Joris surname: Beld fullname: Beld, Joris organization: Department of Chemistry and Biochemistry, University of California, San Diego – sequence: 6 givenname: Jesus F. surname: Barajas fullname: Barajas, Jesus F. organization: Department of Molecular Biology and Biochemistry, University of California, Irvine – sequence: 7 givenname: Joseph J. surname: Hale fullname: Hale, Joseph J. organization: Department of Chemistry and Biochemistry, University of California, San Diego – sequence: 8 givenname: Ray surname: Luo fullname: Luo, Ray organization: Department of Molecular Biology and Biochemistry, University of California, Irvine – sequence: 9 givenname: Michael D. orcidid: 0000-0002-4472-2254 surname: Burkart fullname: Burkart, Michael D. email: mburkart@ucsd.edu organization: Department of Chemistry and Biochemistry, University of California, San Diego – sequence: 10 givenname: Shiou-Chuan surname: Tsai fullname: Tsai, Shiou-Chuan email: sctsai@uci.edu organization: Department of Molecular Biology and Biochemistry, University of California, Irvine, Department of Chemistry, University of California, Irvine, Department of Pharmaceutical Sciences, University of California, Irvine |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31209348$$D View this record in MEDLINE/PubMed |
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| Copyright | The Author(s), under exclusive licence to Springer Nature America, Inc. 2019 Copyright Nature Publishing Group Jul 2019 |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 AUTHOR CONTRIBUTIONS JCM performed the crystallography and structural analysis as well as prepared the manuscript. DJL performed protein NMR, cloning and in vivo complementation, fatty acid analysis, and also prepared the manuscript. DRJ performed crystallography and structural analysis. AJS performed MD simulations and analysis. JB performed synthesis of the crosslinker and fatty acid analysis. JFB performed structural refinement and validation. JJH performed GCMS and analysis. RL provided computational support and supervised MD and dry lab work. MDB supervised protein NMR, fatty acid complementation, and GCMS analysis. SCT supervised crystallography and wet-lab work. All authors contributed to editing the manuscript. |
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| Snippet | Fatty acid synthases are dynamic ensembles of enzymes that can biosynthesize long hydrocarbon chains efficiently. Here we visualize the interaction between the... Fatty acid synthases are dynamic ensembles of enzymes that can efficiently biosynthesize long hydrocarbon chains. Here we visualize the interaction between the... |
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| SubjectTerms | 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase - chemistry 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase - metabolism 631/535/1266 631/535/878 631/92/60 631/92/607 Acyl carrier protein Acyl Carrier Protein - chemistry Acyl Carrier Protein - metabolism Biochemical Engineering Biochemistry Bioorganic Chemistry Brief Communication Cell Biology Chemistry Chemistry and Materials Science Chemistry/Food Science Crystallography Crystallography, X-Ray E coli Escherichia coli - chemistry Escherichia coli - enzymology Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Fatty Acid Synthase, Type II - chemistry Fatty Acid Synthase, Type II - metabolism Fatty acids Lipids Models, Molecular Molecular dynamics NMR Nuclear magnetic resonance Protein Binding Protein interaction Proteins X-ray crystallography |
| Title | Molecular basis for interactions between an acyl carrier protein and a ketosynthase |
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