PMID:12057197

Citation	Roujeinikova, A, Baldock, C, Simon, WJ, Gilroy, J, Baker, PJ, Stuitje, AR, Rice, DW, Slabas, AR and Rafferty, JB (2002) X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site. Structure 10:825-35
Abstract	Acyl carrier protein (ACP) is an essential cofactor in biosynthesis of fatty acids and many other reactions that require acyl transfer steps. We have determined the first crystal structures of an acylated form of ACP from E. coli, that of butyryl-ACP. Our analysis of the molecular surface of ACP reveals a plastic hydrophobic cavity in the vicinity of the phosphopantethylated Ser36 residue that is expanded and occupied by the butyryl and beta-mercaptoethylamine moieties of the acylated 4'-phosphopantetheine group in one of our crystal forms. In the other form, the cavity is contracted, and we propose that the protein has adopted the conformation after delivery of substrate into the active site of a partner enzyme.
Links	PubMed
Keywords	Acyl Carrier Protein/chemistry; Acyl Carrier Protein/metabolism; Binding Sites; Crystallography, X-Ray; Escherichia coli/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Magnetic Resonance Spectroscopy; Models, Molecular; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
ECOLI:ACP	enables	GO:0008289: lipid binding	ECO:0000315: mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
ECOLI:ACP	enables	GO:0000035: acyl binding	ECO:0000315: mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete

References

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