3wgx: Difference between revisions
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<StructureSection load='3wgx' size='340' side='right' caption='[[3wgx]], [[Resolution|resolution]] 0.92Å' scene=''> | <StructureSection load='3wgx' size='340' side='right' caption='[[3wgx]], [[Resolution|resolution]] 0.92Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3wgx]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WGX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WGX FirstGlance]. <br> | <table><tr><td colspan='2'>[[3wgx]] is a 4 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=3WGX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WGX 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></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TLP46 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3wgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgx OCA], [http://pdbe.org/3wgx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wgx RCSB], [http://www.ebi.ac.uk/pdbsum/3wgx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wgx ProSAT]</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=3wgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgx OCA], [http://pdbe.org/3wgx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wgx RCSB], [http://www.ebi.ac.uk/pdbsum/3wgx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wgx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Inaba, K]] | [[Category: Inaba, K]] | ||
[[Category: Kojima, R]] | [[Category: Kojima, R]] | ||
Revision as of 12:09, 21 February 2019
Crystal structure of ERp46 Trx2 in a complex with Prx4 C-termCrystal structure of ERp46 Trx2 in a complex with Prx4 C-term
Structural highlights
Function[TXND5_HUMAN] Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide-isomerase deficiency in yeast (By similarity). [PRDX4_MOUSE] Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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