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PMID:12057197

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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

Significance

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

Notes

See also

References

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