View source for 3llk


==Sulfhydryl Oxidase Fragment of Human QSOX1==
<StructureSection load='3llk' size='340' side='right'caption='[[3llk]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3llk]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LLK FirstGlance]. <br>
</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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3llk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3llk OCA], [https://pdbe.org/3llk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3llk RCSB], [https://www.ebi.ac.uk/pdbsum/3llk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3llk ProSAT]</span></td></tr>
</table>
== Function ==
[https://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/3llk_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3llk ConSurf].
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3llk" style="background-color:#fffaf0;"></div>

==See Also==
*[[Sulfhydryl oxidase 3D structures|Sulfhydryl oxidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Alon A]]
[[Category: Fass D]]