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| | <StructureSection load='3idv' size='340' side='right'caption='[[3idv]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='3idv' size='340' side='right'caption='[[3idv]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3idv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IDV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3idv]] is a 1 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=3IDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IDV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.95Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDIA4, ERP70, ERP72 ([https://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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [https://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=3idv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3idv OCA], [https://pdbe.org/3idv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3idv RCSB], [https://www.ebi.ac.uk/pdbsum/3idv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3idv ProSAT]</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=3idv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3idv OCA], [https://pdbe.org/3idv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3idv RCSB], [https://www.ebi.ac.uk/pdbsum/3idv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3idv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PDIA4_HUMAN PDIA4_HUMAN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Protein disulfide-isomerase]]
| + | [[Category: Gehring K]] |
| - | [[Category: Gehring, K]] | + | [[Category: Kozlov G]] |
| - | [[Category: Kozlov, G]] | + | |
| - | [[Category: Disulfide bond]]
| + | |
| - | [[Category: Endoplasmic reticulum]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Redox-active center]]
| + | |
| - | [[Category: Thioredoxin-like fold]]
| + | |
| Structural highlights
Function
PDIA4_HUMAN
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Protein disulfide isomerases (PDIs) are responsible for catalyzing the proper oxidation and isomerization of disulfide bonds of newly synthesized proteins in the endoplasmic reticulum (ER). The ER contains many different PDI-like proteins. Some, such as PDI, are general enzymes that directly recognize misfolded proteins while others, such as ERp57 and ERp72, have more specialized roles. Here, we report the high-resolution X-ray crystal structure of the N-terminal portion of ERp72 (also known as CaBP2 or PDI A4), which contains two a(0)a catalytic thioredoxin-like domains. The structure shows that the a(0) domain contains an additional N-terminal beta-strand and a different conformation of the beta5-alpha4 loop relative to other thioredoxin-like domains. The structure of the a domain reveals that a conserved arginine residue inserts into the hydrophobic core and makes a salt bridge with a conserved glutamate residue in the vicinity of the catalytic site. A structural model of full-length ERp72 shows that all three catalytic sites roughly face each other and positions the adjacent hydrophobic patches that are likely involved in protein substrate binding.
Structure of the catalytic a(0)a fragment of the protein disulfide isomerase ERp72.,Kozlov G, Azeroual S, Rosenauer A, Maattanen P, Denisov AY, Thomas DY, Gehring K J Mol Biol. 2010 Aug 27;401(4):618-25. Epub 2010 Jun 26. PMID:20600112[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kozlov G, Azeroual S, Rosenauer A, Maattanen P, Denisov AY, Thomas DY, Gehring K. Structure of the catalytic a(0)a fragment of the protein disulfide isomerase ERp72. J Mol Biol. 2010 Aug 27;401(4):618-25. Epub 2010 Jun 26. PMID:20600112 doi:10.1016/j.jmb.2010.06.045
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