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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