1vqw
From Proteopedia
(New page: 200px<br /><applet load="1vqw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vqw, resolution 2.40Å" /> '''Crystal structure of...) |
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| - | [[Image:1vqw.gif|left|200px]]<br /><applet load="1vqw" size=" | + | [[Image:1vqw.gif|left|200px]]<br /><applet load="1vqw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vqw, resolution 2.40Å" /> | caption="1vqw, resolution 2.40Å" /> | ||
'''Crystal structure of a protein with similarity to flavin-containing monooxygenases and to mammalian dimethylalanine monooxygenases'''<br /> | '''Crystal structure of a protein with similarity to flavin-containing monooxygenases and to mammalian dimethylalanine monooxygenases'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Elimination of nonnutritional and insoluble compounds is a critical task | + | 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== | ==About this Structure== | ||
| - | 1VQW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe] with FAD and EPE as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | + | 1VQW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe] with <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=EPE:'>EPE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1YBP. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VQW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Schizosaccharomyces pombe]] | [[Category: Schizosaccharomyces pombe]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
[[Category: Eswaramoorthy, S.]] | [[Category: Eswaramoorthy, S.]] | ||
| - | [[Category: NYSGXRC, New | + | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] |
[[Category: Swaminathan, S.]] | [[Category: Swaminathan, S.]] | ||
[[Category: EPE]] | [[Category: EPE]] | ||
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[[Category: t1729]] | [[Category: t1729]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:37:41 2008'' |
Revision as of 13:37, 21 February 2008
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Crystal structure of a protein with similarity to flavin-containing monooxygenases and to mammalian dimethylalanine monooxygenases
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
1VQW is a Single protein structure of sequence from Schizosaccharomyces pombe with and as ligands. This structure supersedes the now removed PDB entry 1YBP. 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 Thu Feb 21 15:37:41 2008
Categories: Schizosaccharomyces pombe | Single protein | Burley, S K. | Eswaramoorthy, S. | NYSGXRC, New York Structural GenomiX Research Consortium. | Swaminathan, S. | EPE | FAD | Dimer | Flavin-containing | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomics | T1729
