Structural and dynamical rationale for fatty acid unsaturation in Escherichia coli.
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ABSTRACT:
SUBMITTER: Dodge GJ
PROVIDER: S-EPMC6452729 | biostudies-literature | 2019 Apr
REPOSITORIES: biostudies-literature
Publications
Structural and dynamical rationale for fatty acid unsaturation in <i>Escherichia coli</i>.
Dodge Greg J GJ Patel Ashay A Jaremko Kara L KL McCammon J Andrew JA Smith Janet L JL Burkart Michael D MD
Proceedings of the National Academy of Sciences of the United States of America 20190314 14
Fatty acid biosynthesis in α- and γ-proteobacteria requires two functionally distinct dehydratases, FabA and FabZ. Here, mechanistic cross-linking facilitates the structural characterization of a stable hexameric complex of six <i>Escherichia coli</i> 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 demon ...[more]
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