1vqw

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[[Image:1vqw.png|left|200px]]
 
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{{STRUCTURE_1vqw| PDB=1vqw | SCENE= }}
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==Crystal structure of a protein with similarity to flavin-containing monooxygenases and to mammalian dimethylalanine monooxygenases==
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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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===Crystal structure of a protein with similarity to flavin-containing monooxygenases and to mammalian dimethylalanine monooxygenases===
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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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{{ABSTRACT_PUBMED_16777962}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 1vqw" style="background-color:#fffaf0;"></div>
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[[1vqw]] is a 2 chain structure with sequence from [http://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].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:016777962</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe]]
[[Category: Schizosaccharomyces pombe]]
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[[Category: Burley, S K.]]
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[[Category: Burley SK]]
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[[Category: Eswaramoorthy, S.]]
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[[Category: Eswaramoorthy S]]
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[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics.]]
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[[Category: Swaminathan S]]
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[[Category: Swaminathan, S.]]
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[[Category: Dimer]]
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[[Category: Flavin-containing]]
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[[Category: New york sgx research center for structural genomic]]
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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 genomic]]
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[[Category: T1729]]
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[[Category: Unknown function]]
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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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