期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 365, 期 1, 页码 135-145出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2006.09.049
关键词
acyl carrier protein; fatty acid biosynthesis; acyl chain binding; hydrophobic binding pocket; conformational changes
资金
- Biotechnology and Biological Sciences Research Council [BB/D524975/1] Funding Source: Medline
- Biotechnology and Biological Sciences Research Council [BB/D524975/1] Funding Source: researchfish
- BBSRC [BB/D524975/1] Funding Source: UKRI
A knowledge of the structures of acyl chain loaded species of the acyl carrier protein (ACP) as used in fatty acid biosynthesis and a range of other metabolic events, is essential for a full understanding of the molecular recognition at the heart of these processes. To date the only crystal structure of an acylated species of ACP is that of a butyryl derivative of Escherichia coli ACP. We have now determined the structures of a family of acylated E. coli ACPs of varying acyl chain length. The acyl moiety is attached via a thioester bond to a phosphopantetheine linker that is in turn bound to a serine residue in ACdP. The growing acyl chain can be accommodated within a central cavity in the ACP for transport during the elongation stages of lipid synthesis through changes in the conformation of a four alpha-helix bundle. The results not only clarify the means by which a substrate of varying size and complexity is transported in the cell but also suggest a mechanism by which interacting enzymes can recognize the loaded ACP through recognition of surface features including the conformation of the phosphopantetheine linker.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据