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| | <StructureSection load='4p2l' size='340' side='right'caption='[[4p2l]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='4p2l' size='340' side='right'caption='[[4p2l]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4p2l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P2L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P2L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4p2l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P2L 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t58|3t58]], [[3q6o|3q6o]], [[3llk|3llk]], [[3qcp|3qcp]]</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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Qsox1, Qscn6, Sox2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=4p2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p2l OCA], [https://pdbe.org/4p2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p2l RCSB], [https://www.ebi.ac.uk/pdbsum/4p2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p2l ProSAT]</span></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=4p2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p2l OCA], [http://pdbe.org/4p2l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p2l RCSB], [http://www.ebi.ac.uk/pdbsum/4p2l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p2l ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/QSOX1_RAT QSOX1_RAT]] 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.<ref>PMID:16806532</ref> | + | [https://www.uniprot.org/uniprot/QSOX1_RAT QSOX1_RAT] 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.<ref>PMID:16806532</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Sulfhydryl oxidase|Sulfhydryl oxidase]] | + | *[[Sulfhydryl oxidase 3D structures|Sulfhydryl oxidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thiol oxidase]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Fass, D]] | + | [[Category: Fass D]] |
| - | [[Category: Gat, Y]] | + | [[Category: Gat Y]] |
| - | [[Category: Disulfide formation]]
| + | |
| - | [[Category: Enzyme intermediate]]
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| - | [[Category: Erv fold]]
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| - | [[Category: Oxidoreductase]]
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| - | [[Category: Thioredoxin fold]]
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| Structural highlights
Function
QSOX1_RAT 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.[1]
Publication Abstract from PubMed
Thioredoxin superfamily proteins introduce disulfide bonds into substrates, catalyze the removal of disulfides, and operate in electron relays. These functions rely on one or more dithiol/disulfide exchange reactions. The flavoenzyme quiescin sulfhydryl oxidase (QSOX), a catalyst of disulfide bond formation with an interdomain electron transfer step in its catalytic cycle, provides a unique opportunity for exploring the structural environment of enzymatic dithiol/disulfide exchange. Wild-type Rattus norvegicus QSOX1 (RnQSOX1) was crystallized in a conformation that juxtaposes the two redox-active di-cysteine motifs in the enzyme, presenting the entire electron-transfer pathway and proton-transfer participants in their native configurations. As such a state cannot generally be enriched and stabilized for analysis, RnQSOX1 gives unprecedented insight into the functional group environments of the four cysteines involved in dithiol/disulfide exchange and provides the framework for analysis of the energetics of electron transfer in the presence of the bound flavin adenine dinucleotide cofactor. Hybrid quantum mechanics/molecular mechanics (QM/MM) free energy simulations based on the X-ray crystal structure suggest that formation of the interdomain disulfide intermediate is highly favorable and secures the flexible enzyme in a state from which further electron transfer via the flavin can occur.
Enzyme structure captures four cysteines aligned for disulfide relay.,Gat Y, Vardi-Kilshtain A, Grossman I, Major DT, Fass D Protein Sci. 2014 Jun 3. doi: 10.1002/pro.2496. PMID:24888638[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Radom J, Colin D, Thiebault F, Dognin-Bergeret M, Mairet-Coello G, Esnard-Feve A, Fellmann D, Jouvenot M. Identification and expression of a new splicing variant of FAD-sulfhydryl oxidase in adult rat brain. Biochim Biophys Acta. 2006 May;1759(5):225-33. Epub 2006 May 9. PMID:16806532 doi:http://dx.doi.org/10.1016/j.bbaexp.2006.04.008
- ↑ Gat Y, Vardi-Kilshtain A, Grossman I, Major DT, Fass D. Enzyme structure captures four cysteines aligned for disulfide relay. Protein Sci. 2014 Jun 3. doi: 10.1002/pro.2496. PMID:24888638 doi:http://dx.doi.org/10.1002/pro.2496
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