2gv8

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Revision as of 18:08, 29 January 2008

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spinqualitylabelsall models 2gv8, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

2GV8 is a Single protein structure of sequence from Schizosaccharomyces pombe with , and as ligands. Full crystallographic information is available from OCA.

Reference

Mechanism of action of a flavin-containing monooxygenase., Eswaramoorthy S, Bonanno JB, Burley SK, Swaminathan S, Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):9832-7. Epub 2006 Jun 15. PMID:16777962

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