6n3p | pdb_00006n3p

Crosslinked AcpP=FabZ complex from E. coli Type II FAS

spinqualitylabelsall models 6n3p, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6n3p is a 12 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: XLN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FABZ_ECOLI Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acyl carrier protein 3D structures Beta-hydroxyacyl-acyl carrier protein dehydratase 3D structures

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