3lli
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3lli is ON HOLD Authors: Alon, A., Heckler, E.J., Thorpe, C., Fass, D. Description: Sulfhydryl Oxidase Fragment of Human QSOX1 ''Page seeded by [h...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Sulfhydryl Oxidase Fragment of Human QSOX1== | |
| + | <StructureSection load='3lli' size='340' side='right' caption='[[3lli]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3lli]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LLI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LLI FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jr8|1jr8]], [[1jra|1jra]], [[2hj3|2hj3]], [[3gwn|3gwn]], [[3gwl|3gwl]], [[1oqc|1oqc]], [[3llk|3llk]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">QSCN6, QSOX1, UNQ2520/PRO6013 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiol_oxidase Thiol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lli OCA], [http://pdbe.org/3lli PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lli RCSB], [http://www.ebi.ac.uk/pdbsum/3lli PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lli ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/QSOX1_HUMAN QSOX1_HUMAN]] Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins. In fibroblasts, it may have tumor-suppressing capabilities being involved in growth regulation.<ref>PMID:16806532</ref> <ref>PMID:10542195</ref> <ref>PMID:10708601</ref> <ref>PMID:12176051</ref> <ref>PMID:17331072</ref> <ref>PMID:18393449</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/3lli_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=3lli ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Quiescin sulfhydryl oxidase (QSOX) catalyzes formation of disulfide bonds between cysteine residues in substrate proteins. Human QSOX1 is a multi-domain, monomeric enzyme containing a module related to the single-domain sulfhydryl oxidases of the Erv family. A partial QSOX1 crystal structure reveals a single-chain pseudo-dimer mimicking the quaternary structure of Erv enzymes. However, one pseudo-dimer "subunit" has lost its cofactor and catalytic activity. In QSOX evolution, a further concatenation to a member of the protein disulfide isomerase family resulted in an enzyme capable of both disulfide formation and efficient transfer to substrate proteins. | ||
| - | + | QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains.,Alon A, Heckler EJ, Thorpe C, Fass D FEBS Lett. 2010 Apr 16;584(8):1521-5. Epub 2010 Mar 6. PMID:20211621<ref>PMID:20211621</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3lli" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Sulfhydryl oxidase|Sulfhydryl oxidase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Thiol oxidase]] | ||
| + | [[Category: Alon, A]] | ||
| + | [[Category: Fass, D]] | ||
| + | [[Category: Disulfide]] | ||
| + | [[Category: Fad]] | ||
| + | [[Category: Flavin adenine dinucleotide]] | ||
| + | [[Category: Flavoprotein]] | ||
| + | [[Category: Glycoprotein]] | ||
| + | [[Category: Golgi apparatus]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Secreted]] | ||
| + | [[Category: Sulfhydryl oxidase]] | ||
Current revision
Sulfhydryl Oxidase Fragment of Human QSOX1
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