1vqw

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(New page: 200px<br /><applet load="1vqw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vqw, resolution 2.40&Aring;" /> '''Crystal structure of...)
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[[Image:1vqw.gif|left|200px]]<br /><applet load="1vqw" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1vqw, resolution 2.40&Aring;" />
 
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'''Crystal structure of a protein with similarity to flavin-containing monooxygenases and to mammalian dimethylalanine monooxygenases'''<br />
 
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==Overview==
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==Crystal structure of a protein with similarity to flavin-containing monooxygenases and to mammalian dimethylalanine monooxygenases==
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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.
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<StructureSection load='1vqw' size='340' side='right'caption='[[1vqw]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1vqw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ybp 1ybp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VQW FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vqw OCA], [https://pdbe.org/1vqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vqw RCSB], [https://www.ebi.ac.uk/pdbsum/1vqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vqw ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1vqw TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FMO1_SCHPO FMO1_SCHPO] Flavin-dependent oxidation of thiol-containing compounds. Probably required for the correct folding of disulfide-bonded proteins (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vq/1vqw_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vqw ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:16777962</ref>
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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 superseeds the now removed PDB entry 1YBP. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VQW OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16777962 16777962]
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</div>
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<div class="pdbe-citations 1vqw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe]]
[[Category: Schizosaccharomyces pombe]]
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[[Category: Single protein]]
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[[Category: Burley SK]]
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[[Category: Burley, S.K.]]
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[[Category: Eswaramoorthy S]]
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[[Category: Eswaramoorthy, S.]]
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[[Category: Swaminathan S]]
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[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
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[[Category: Swaminathan, S.]]
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[[Category: EPE]]
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[[Category: FAD]]
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[[Category: dimer]]
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[[Category: flavin-containing]]
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[[Category: new york structural genomix research consortium]]
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[[Category: nysgxrc]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: structural genomics]]
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[[Category: t1729]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:02:59 2007''
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Current revision

Crystal structure of a protein with similarity to flavin-containing monooxygenases and to mammalian dimethylalanine monooxygenases

PDB ID 1vqw

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