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 Nature Publishing Group
Schlagworte:	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
ISSN:	1552-4450, 1552-4469, 1552-4469
Online-Zugang:	Volltext
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Beschreibung
Zusammenfassung:	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.
Bibliographie:	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.
ISSN:	1552-4450 1552-4469 1552-4469
DOI:	10.1038/s41589-019-0301-y