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3ieg
From Proteopedia
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| - | {{STRUCTURE_3ieg| PDB=3ieg | SCENE= }} | ||
| - | ===Crystal Structure of P58(IPK) TPR Domain at 2.5 A=== | ||
| - | {{ABSTRACT_PUBMED_20184891}} | ||
| - | == | + | ==Crystal Structure of P58(IPK) TPR Domain at 2.5 A== |
| - | [[3ieg]] is a 2 chain structure with sequence from [ | + | <StructureSection load='3ieg' size='340' side='right'caption='[[3ieg]], [[Resolution|resolution]] 2.51Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ieg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IEG FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dnajc3, P58(IPK), P58ipk ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3ieg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ieg OCA], [https://pdbe.org/3ieg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ieg RCSB], [https://www.ebi.ac.uk/pdbsum/3ieg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ieg ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ie/3ieg_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ieg ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | P58(IPK) might function as an endoplasmic reticulum molecular chaperone to maintain protein folding homeostasis during unfolded protein responses. P58(IPK) contains nine tetratricopeptide repeat (TPR) motifs and a C-terminal J-domain within its primary sequence. To investigate the mechanism by which P58(IPK) functions to promote protein folding within the endoplasmic reticulum, we have determined the crystal structure of P58(IPK) TPR fragment to 2.5 A resolution by the SAD method. The crystal structure of P58(IPK) revealed three domains (I-III) with similar folds and each domain contains three TPR motifs. An ELISA assay indicated that P58(IPK) acts as a molecular chaperone by interacting with misfolded proteins such as luciferase and rhodanese. The P58(IPK) structure reveals a conserved hydrophobic patch located in domain I that might be involved in binding the misfolded polypeptides. Structure-based mutagenesis for the conserved hydrophobic residues located in domain I significantly reduced the molecular chaperone activity of P58(IPK). | ||
| - | + | Crystal structure of P58(IPK) TPR fragment reveals the mechanism for its molecular chaperone activity in UPR.,Tao J, Petrova K, Ron D, Sha B J Mol Biol. 2010 Apr 16;397(5):1307-15. Epub 2010 Feb 22. PMID:20184891<ref>PMID:20184891</ref> | |
| - | <ref | + | |
| - | [[Category: | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | [[Category: Sha, B | + | </div> |
| - | [[Category: Tao, J | + | <div class="pdbe-citations 3ieg" style="background-color:#fffaf0;"></div> |
| + | |||
| + | ==See Also== | ||
| + | *[[DnaJ homolog 3D structures|DnaJ homolog 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lk3 transgenic mice]] | ||
| + | [[Category: Sha, B]] | ||
| + | [[Category: Tao, J]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Endoplasmic reticulum]] | [[Category: Endoplasmic reticulum]] | ||
Current revision
Crystal Structure of P58(IPK) TPR Domain at 2.5 A
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