2gv8
From Proteopedia
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'''Crystal structure of flavin-containing monooxygenase (FMO) from S.pombe and NADPH cofactor complex''' | '''Crystal structure of flavin-containing monooxygenase (FMO) from S.pombe and NADPH cofactor complex''' | ||
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[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] | ||
[[Category: Swaminathan, S.]] | [[Category: Swaminathan, S.]] | ||
| - | [[Category: | + | [[Category: Cofactor complex]] |
| - | [[Category: | + | [[Category: Fad]] |
| - | [[Category: | + | [[Category: Fmo]] |
| - | [[Category: | + | [[Category: Nadph]] |
| - | [[Category: | + | [[Category: New york structural genomix research consortium]] |
| - | [[Category: | + | [[Category: Nysgxrc]] |
| - | [[Category: | + | [[Category: Oxygenase]] |
| - | [[Category: | + | [[Category: Protein structure initiative]] |
| - | [[Category: | + | [[Category: Psi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:34:43 2008'' | |
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Revision as of 02:34, 4 May 2008
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. 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 Page seeded by OCA on Sun May 4 05:34:43 2008
Categories: Schizosaccharomyces pombe | Single protein | Burley, S K. | Eswaramoorthy, S. | NYSGXRC, New York Structural GenomiX Research Consortium. | Swaminathan, S. | Cofactor complex | Fad | Fmo | Nadph | New york structural genomix research consortium | Nysgxrc | Oxygenase | Protein structure initiative | Psi | Structural genomic
