4p2l: Difference between revisions
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''' | ==Quiescin Sulfhydryl Oxidase from Rattus norvegicus== | ||
<StructureSection load='4p2l' size='340' side='right' caption='[[4p2l]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4p2l]] is a 2 chain structure. 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> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t58|3t58]], [[3q6o|3q6o]], [[3llk|3llk]], [[3qcp|3qcp]]</td></tr> | |||
<tr><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><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://www.rcsb.org/pdb/explore.do?structureId=4p2l RCSB], [http://www.ebi.ac.uk/pdbsum/4p2l PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:24888638</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Thiol oxidase]] | |||
[[Category: Fass, D.]] | |||
[[Category: Gat, Y.]] | |||
[[Category: Disulfide formation]] | |||
[[Category: Enzyme intermediate]] | |||
[[Category: Erv fold]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Thioredoxin fold]] | |||
Revision as of 06:27, 25 June 2014
Quiescin Sulfhydryl Oxidase from Rattus norvegicus
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