View source for 3wgd


==Crystal structure of ERp46 Trx1==
<StructureSection load='3wgd' size='340' side='right' caption='[[3wgd]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wgd]] is a 9 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WGD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WGD FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wge|3wge]]</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=3wgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgd OCA], [http://pdbe.org/3wgd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wgd RCSB], [http://www.ebi.ac.uk/pdbsum/3wgd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wgd ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/TXND5_HUMAN TXND5_HUMAN]] Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide-isomerase deficiency in yeast (By similarity). 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The mammalian endoplasmic reticulum (ER) contains a diverse oxidative protein folding network in which ERp46, a member of the protein disulfide isomerase (PDI) family, serves as an efficient disulfide bond introducer together with Peroxiredoxin-4 (Prx4). We revealed a radically different molecular architecture of ERp46, in which the N-terminal two thioredoxin (Trx) domains with positively charged patches near their peptide-binding site and the C-terminal Trx are linked by unusually long loops and arranged extendedly, forming an opened V-shape. Whereas PDI catalyzes native disulfide bond formation by the cooperative action of two mutually facing redox-active sites on folding intermediates bound to the central cleft, ERp46 Trx domains are separated, act independently, and engage in rapid but promiscuous disulfide bond formation during early oxidative protein folding. Thus, multiple PDI family members likely contribute to different stages of oxidative folding and work cooperatively to ensure the efficient production of multi-disulfide proteins in the ER.

Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family.,Kojima R, Okumura M, Masui S, Kanemura S, Inoue M, Saiki M, Yamaguchi H, Hikima T, Suzuki M, Akiyama S, Inaba K Structure. 2014 Mar 4;22(3):431-43. doi: 10.1016/j.str.2013.12.013. Epub 2014 Jan, 23. PMID:24462249<ref>PMID:24462249</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wgd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Inaba, K]]
[[Category: Kojima, R]]
[[Category: Suzuki, M]]
[[Category: Isomerase]]
[[Category: Pdi family member]]
[[Category: Protein disulfide isomerase]]
[[Category: Thioredoxin domain]]