6b2t | pdb_00006b2t

Crystal structure of Xanthomonas campestris OleA H285D

spinqualitylabelsall models 6b2t, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6b2t is a 2 chain structure with sequence from Xancp. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, PO4 NonStd Res: CSO Gene: fabH, XCC0212 (XANCP) Activity: [acyl-carrier-protein_synthase_I Beta-ketoacyl-[acyl-carrier-protein] synthase I], with EC number 2.3.1.41 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Renewable production of hydrocarbons is being pursued as a petroleum-independent source of commodity chemicals and replacement for biofuels. The bacterial biosynthesis of long-chain olefins represents one such platform. The process is initiated by OleA catalyzing the condensation of two fatty acyl-coenzyme A substrates to form a beta-keto acid. Here, the mechanistic role of the conserved His285 is investigated through mutagenesis, activity assays, and X-ray crystallography. Our data demonstrate that His285 is required for product formation, influences the thiolase nucleophile Cys143 and the acyl-enzyme intermediate before and after transesterification, and orchestrates substrate coordination as a defining component of an oxyanion hole. As a consequence, His285 plays a key role in enabling a mechanistic strategy in OleA that is distinct from other thiolases. The role of OleA His285 in orchestration of long-chain acyl-coenzyme A substrates.,Jensen MR, Goblirsch BR, Esler MA, Christenson JK, Mohamed FA, Wackett LP, Wilmot CM FEBS Lett. 2018 Feb 11. doi: 10.1002/1873-3468.13004. PMID:29430657 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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