2GVC
Crystal structure of flavin-containing monooxygenase (FMO)from S.pombe and substrate (methimazole) complex
Summary for 2GVC
| Entry DOI | 10.2210/pdb2gvc/pdb |
| Related | 1VQW 2GV8 |
| Descriptor | monooxygenase, HYDROGEN PEROXIDE, FLAVIN-ADENINE DINUCLEOTIDE, ... (6 entities in total) |
| Functional Keywords | fmo, fad, methimazole, oxygenase, psi, structural genomics, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, oxidoreductase |
| Biological source | Schizosaccharomyces pombe (fission yeast) |
| Total number of polymer chains | 4 |
| Total formula weight | 204821.48 |
| Authors | Eswaramoorthy, S.,Swaminathan, S.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2006-05-02, release date: 2006-06-06, Last modification date: 2023-11-15) |
| Primary citation | 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 Cited by 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: 16777962DOI: 10.1073/pnas.0602398103 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.22 Å) |
Structure validation
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