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
Hauptverfasser: Milligan, Jacob C., Lee, D. John, Jackson, David R., Schaub, Andrew J., Beld, Joris, Barajas, Jesus F., Hale, Joseph J., Luo, Ray, Burkart, Michael D., Tsai, Shiou-Chuan
Format: Journal Article
Sprache:Englisch
Veröffentlicht: New York Nature Publishing Group US 01.07.2019
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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
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  surname: Schaub
  fullname: Schaub, Andrew J.
  organization: Department of Chemistry, University of California, Irvine
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  surname: Beld
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  organization: Department of Chemistry and Biochemistry, University of California, San Diego
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  organization: Department of Molecular Biology and Biochemistry, University of California, Irvine
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  surname: Hale
  fullname: Hale, Joseph J.
  organization: Department of Chemistry and Biochemistry, University of California, San Diego
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  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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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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StartPage 669
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
URI https://link.springer.com/article/10.1038/s41589-019-0301-y
https://www.ncbi.nlm.nih.gov/pubmed/31209348
https://www.proquest.com/docview/2246226458
https://www.proquest.com/docview/2242828284
https://pubmed.ncbi.nlm.nih.gov/PMC7323458
Volume 15
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