Structural highlights
Function
[FABZ_ECO45] Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. [ACP_ECO45] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217]
Publication Abstract from PubMed
Fatty acid biosynthesis in alpha- and gamma-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.
Structural and dynamical rationale for fatty acid unsaturation in Escherichia coli.,Dodge GJ, Patel A, Jaremko KL, McCammon JA, Smith JL, Burkart MD Proc Natl Acad Sci U S A. 2019 Mar 14. pii: 1818686116. doi:, 10.1073/pnas.1818686116. PMID:30872475[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dodge GJ, Patel A, Jaremko KL, McCammon JA, Smith JL, Burkart MD. Structural and dynamical rationale for fatty acid unsaturation in Escherichia coli. Proc Natl Acad Sci U S A. 2019 Mar 14. pii: 1818686116. doi:, 10.1073/pnas.1818686116. PMID:30872475 doi:http://dx.doi.org/10.1073/pnas.1818686116
