8T3P

Crystal structure of MonC1 (a flavin-dependent monooxygenase)

8T3P の概要

• エントリーDOI: 10.2210/pdb8t3p/pdb
• 分子名称: MonCI, FLAVIN-ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: monc1, flavin-dependent monooxygenase, oxidoreductase
• 由来する生物種: Streptomyces virginiae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 112148.61

構造登録者

Wang, Q.,Mathews, I.I.,Kim, C.Y. (登録日: 2023-06-07, 公開日: 2023-11-08)

主引用文献

Wang, Q.,Liu, N.,Deng, Y.,Guan, Y.,Xiao, H.,Nitka, T.A.,Yang, H.,Yadav, A.,Vukovic, L.,Mathews, I.I.,Chen, X.,Kim, C.Y.
Triepoxide formation by a flavin-dependent monooxygenase in monensin biosynthesis.
Nat Commun, 14:6273-6273, 2023

PubMed Abstract: Monensin A is a prototypical natural polyether polyketide antibiotic. It acts by binding a metal cation and facilitating its transport across the cell membrane. Biosynthesis of monensin A involves construction of a polyene polyketide backbone, subsequent epoxidation of the alkenes, and, lastly, formation of cyclic ethers via epoxide-opening cyclization. MonCI, a flavin-dependent monooxygenase, is thought to transform all three alkenes in the intermediate polyketide premonensin A into epoxides. Our crystallographic study has revealed that MonCI's exquisite stereocontrol is due to the preorganization of the active site residues which allows only one specific face of the alkene to approach the reactive C(4a)-hydroperoxyflavin moiety. Furthermore, MonCI has an unusually large substrate-binding cavity that can accommodate premonensin A in an extended or folded conformation which allows any of the three alkenes to be placed next to C(4a)-hydroperoxyflavin. MonCI, with its ability to perform multiple epoxidations on the same substrate in a stereospecific manner, demonstrates the extraordinary versatility of the flavin-dependent monooxygenase family of enzymes.

PubMed: 37805629
DOI: 10.1038/s41467-023-41889-0

実験手法

X-RAY DIFFRACTION (1.9 Å)