6jdk

Crystal structure of Baeyer-Villiger monooxygenase from Parvibaculum lavamentivoransCrystal structure of Baeyer-Villiger monooxygenase from Parvibaculum lavamentivorans

Structural highlights 6jdk is a 2 chain structure with sequence from Parvibaculum lavamentivorans DS-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.495Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BVMO_PARL1 Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters or lactones using NADPH as an electron donor. Besides cycloalkanones, can use cyclic alpha,beta-unsaturated ketones as substrates, leading to enol-lactones. Can also act on methylated cycloalkanones and methylated cycloalkenones with high enantioselectivity in some cases. Publication Abstract from PubMed Baeyer-Villiger monooxygenase (BVMO) catalyzes insertion of an oxygen atom into aliphatic or cyclic ketones with high regioselectivity. The BVMOs from Parvibaculum lavamentivorans (BVMOParvi) and Oceanicola batsensis (BVMOOcean) are interesting because of their homologies, with >40% sequence identity, and reaction with the same cyclic ketones with a methyl moiety to give different products. The revealed BVMOParvi structure shows that BVMOParvi forms a two-domain structure like other BVMOs. It has two inserted residues, compared with BVMOOcean, that form a bulge near the bound flavin adenine dinucleotide in the active site. Furthermore, this bulge is linked to a nearby alpha-helix via a disulfide bond, probably restricting access of the bulky methyl group of the substrate to this bulge. Another sequence motif at the entrance of the active site (Ala-Ser in BVMOParvi and Ser-Thr in BVMOOcean) allows a large volume in BVMOParvi. These minute differences may discriminate a substrate orientation in both BVMOs from the initial substrate binding pocket to the final oxygenation site, resulting in the inserted oxygen atom being in different positions of the same substrate. Structural basis for the selective addition of an oxygen atom to cyclic ketones by Baeyer-Villiger monooxygenase from Parvibaculum lavamentivorans.,Nguyen TD, Choi GE, Gu DH, Seo PW, Kim JW, Park JB, Kim JS Biochem Biophys Res Commun. 2019 Mar 23. pii: S0006-291X(19)30505-4. doi:, 10.1016/j.bbrc.2019.03.114. PMID:30914200 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monooxygenase 3D structures

spinqualitylabelsall models 6jdk, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image