期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 116, 期 14, 页码 6775-6783出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1818686116
关键词
de novo unsaturated fatty acid biosynthesis; cell membrane homeostasis; chemical biology; structural biology; computational biology
资金
- NIH [GM31749, GM095970, DK042303]
- National Biomedical Computation Resource
- SDSC
- federal funds from the National Institute of General Medical Sciences (GM) [AGM-12006]
- National Cancer Institute (CA) [ACB-12002]
- DOE Office of Science [DE-AC02-06CH11357]
Fatty acid biosynthesis in a- and y-proteobacteria requires two functionally distinct dehydratases, FabA and FabZ. Here, mechanistic cross-linking facilitates the structural characterization of a stable hexameric complex of six Escherichia coli FabZ dehydratase subunits with six AcpP acyl carrier proteins. The crystal structure sheds light on the divergent substrate selectivity of FabA and FabZ by revealing distinct architectures of the binding pocket. Molecular dynamics simulations demonstrate differential biasing of substrate orientations and conformations within the active sites of FabA and FabZ such that FabZ is preorganized to catalyze only dehydration, while FabA is primed for both dehydration and isomerization.
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