期刊
PROTEIN SCIENCE
卷 18, 期 1, 页码 240-246出版社
WILEY-BLACKWELL
DOI: 10.1002/pro.11
关键词
acyl carrier protein; type II fatty acid synthase; NMR; protein structure
资金
- American Lebanese Syrian Associated Charities
- National Institutes of Heath
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM069916, R01GM081492] Funding Source: NIH RePORTER
Fatty acid synthesis in bacteria is catalyzed by a set of individual enzymes known as the type II fatty acid synthase. Acyl carrier protein (ACP) shuttles the acyl intermediates between individual pathway enzymes. In this study, we determined the solution structures of three different forms of ACP, apo-ACP, ACP, and butyryl-ACP under identical experimental conditions. The structural studies revealed that attachment of butyryl acyl intermediate to ACP alters the conformation of ACP. This finding supports the more general notion that the attachment of different acyl intermediates alters the ACP structure to facilitate their recognition and turnover by the appropriate target enzymes.
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