6JDK

Crystal structure of Baeyer-Villiger monooxygenase from Parvibaculum lavamentivorans

6JDK の概要

• エントリーDOI: 10.2210/pdb6jdk/pdb
• 分子名称: Baeyer-Villiger monooxygenase, FLAVIN-ADENINE DINUCLEOTIDE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: monooxygenase, oxidoreductase
• 由来する生物種: Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 125321.06

構造登録者

Kim, J.-S.,Nguyen, T.D. (登録日: 2019-02-01, 公開日: 2019-04-10, 最終更新日: 2024-10-23)

主引用文献

Nguyen, T.D.,Choi, G.E.,Gu, D.H.,Seo, P.W.,Kim, J.W.,Park, J.B.,Kim, J.S.
Structural basis for the selective addition of an oxygen atom to cyclic ketones by Baeyer-Villiger monooxygenase from Parvibaculum lavamentivorans.
Biochem. Biophys. Res. Commun., 512:564-570, 2019

PubMed Abstract: Baeyer-Villiger monooxygenase (BVMO) catalyzes insertion of an oxygen atom into aliphatic or cyclic ketones with high regioselectivity. The BVMOs from Parvibaculum lavamentivorans (BVMO) and Oceanicola batsensis (BVMO) 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 BVMO structure shows that BVMO forms a two-domain structure like other BVMOs. It has two inserted residues, compared with BVMO, that form a bulge near the bound flavin adenine dinucleotide in the active site. Furthermore, this bulge is linked to a nearby α-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 BVMO and Ser-Thr in BVMO) allows a large volume in BVMO. 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.

PubMed: 30914200
DOI: 10.1016/j.bbrc.2019.03.114

実験手法

X-RAY DIFFRACTION (2.495 Å)