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| | ==Crystal structure of the third catalytic domain of ERp46== | | ==Crystal structure of the third catalytic domain of ERp46== |
| - | <StructureSection load='3uvt' size='340' side='right' caption='[[3uvt]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3uvt' size='340' side='right'caption='[[3uvt]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3uvt]] is a 5 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=3UVT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UVT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3uvt]] is a 5 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=3UVT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UVT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TXNDC5, TLP46, UNQ364/PRO700 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></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=3uvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uvt OCA], [https://pdbe.org/3uvt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uvt RCSB], [https://www.ebi.ac.uk/pdbsum/3uvt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uvt 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=3uvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uvt OCA], [http://pdbe.org/3uvt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3uvt RCSB], [http://www.ebi.ac.uk/pdbsum/3uvt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3uvt ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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). | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Protein disulfide-isomerase]] | + | [[Category: Large Structures]] |
| - | [[Category: Gehring, K]] | + | [[Category: Gehring K]] |
| - | [[Category: Gulerez, I E]] | + | [[Category: Gulerez IE]] |
| - | [[Category: Kozlov, G]] | + | [[Category: Kozlov G]] |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Thioredoxin-like fold]]
| + | |
| 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).
Publication Abstract from PubMed
Protein disulfide isomerases are responsible for catalyzing the proper oxidation and isomerization of disulfide bonds of newly synthesized proteins in the endoplasmic reticulum. Here, the crystal structure of the third catalytic domain of protein disulfide isomerase ERp46 (also known as protein disulfide isomerase A5 and TXNDC5) was determined to 2.0 A resolution. The structure shows a typical thioredoxin-like fold, but also identifies regions of high structural variability. In particular, the loop between helix alpha2 and strand beta3 adopts strikingly different conformations among the five chains of the asymmetric unit. Cys381 and Cys388 form a structural disulfide and its absence in one of the molecules leads to dramatic conformational changes. The tryptophan residue Trp349 of this molecule inserts into the cavity formed by helices alpha1 and alpha3 of a neighbouring molecule, potentially mimicking the interactions of ERp46 with misfolded substrates.
Structure of the third catalytic domain of the protein disulfide isomerase ERp46.,Gulerez IE, Kozlov G, Rosenauer A, Gehring K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Apr 1;68(Pt 4):378-81., Epub 2012 Mar 27. PMID:22505402[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gulerez IE, Kozlov G, Rosenauer A, Gehring K. Structure of the third catalytic domain of the protein disulfide isomerase ERp46. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Apr 1;68(Pt 4):378-81., Epub 2012 Mar 27. PMID:22505402 doi:10.1107/S1744309112005866
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