2GVC

Crystal structure of flavin-containing monooxygenase (FMO)from S.pombe and substrate (methimazole) complex

2GVC の概要

• エントリーDOI: 10.2210/pdb2gvc/pdb
• 関連するPDBエントリー: 1VQW 2GV8
• 分子名称: monooxygenase, HYDROGEN PEROXIDE, FLAVIN-ADENINE DINUCLEOTIDE, ... (6 entities in total)
• 機能のキーワード: fmo, fad, methimazole, oxygenase, psi, structural genomics, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, oxidoreductase
• 由来する生物種: Schizosaccharomyces pombe (fission yeast)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 204821.48

構造登録者

Eswaramoorthy, S.,Swaminathan, S.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (登録日: 2006-05-02, 公開日: 2006-06-06, 最終更新日: 2024-11-13)

主引用文献

Eswaramoorthy, S.,Bonanno, J.B.,Burley, S.K.,Swaminathan, S.
Mechanism of action of a flavin-containing monooxygenase.
Proc.Natl.Acad.Sci.Usa, 103:9832-9837, 2006

PubMed Abstract: Elimination of nonnutritional and insoluble compounds is a critical task for any living organism. Flavin-containing monooxygenases (FMOs) attach an oxygen atom to the insoluble nucleophilic compounds to increase solubility and thereby increase excretion. Here we analyze the functional mechanism of FMO from Schizosaccharomyces pombe using the crystal structures of the wild type and protein-cofactor and protein-substrate complexes. The structure of the wild-type FMO revealed that the prosthetic group FAD is an integral part of the protein. FMO needs NADPH as a cofactor in addition to the prosthetic group for its catalytic activity. Structures of the protein-cofactor and protein-substrate complexes provide insights into mechanism of action. We propose that FMOs exist in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor, readying them to act on substrates. The 4alpha-hydroperoxyflavin form of the prosthetic group represents a transient intermediate of the monooxygenation process. The oxygenated and reduced forms of the prosthetic group help stabilize interactions with cofactor and substrate alternately to permit continuous enzyme turnover.

PubMed: 16777962
DOI: 10.1073/pnas.0602398103

実験手法

X-RAY DIFFRACTION (2.22 Å)