X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site

被引:110
作者
Roujeinikova, A
Baldock, C
Simon, WJ
Gilroy, J
Baker, PJ
Stuitje, AR
Rice, DW
Slabas, AR [1 ]
Rafferty, JB
机构
[1] Univ Sheffield, Dept Mol Biol & Biotechnol, Krebs Inst Biomol Res, Sheffield S10 2TN, S Yorkshire, England
[2] Univ Durham, Dept Biol Sci, Durham DH1 3LE, England
[3] Free Univ Amsterdam, Bioctr, Inst Mol Biol Sci, IMBW, NL-1081 HV Amsterdam, Netherlands
基金
英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词
acyl carrier protein; acyl chain binding; crystal structure; fatty acid biosynthesis; binding pocket; conformational changes;
D O I
10.1016/S0969-2126(02)00775-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:825 / 835
页数:11
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