1n57
From Proteopedia
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- | [[Image:1n57.png|left|200px]] | ||
- | + | ==Crystal Structure of Chaperone Hsp31== | |
- | + | <StructureSection load='1n57' size='340' side='right'caption='[[1n57]], [[Resolution|resolution]] 1.60Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[1n57]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N57 FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1n57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n57 OCA], [https://pdbe.org/1n57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n57 RCSB], [https://www.ebi.ac.uk/pdbsum/1n57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n57 ProSAT]</span></td></tr> |
- | [[1n57]] is a 1 chain structure with sequence from [ | + | </table> |
- | + | == Function == | |
- | == | + | [https://www.uniprot.org/uniprot/HCHA_ECOLI HCHA_ECOLI] Functions as a holding molecular chaperone (holdase) which stabilizes unfolding intermediates and rapidly releases them in an active form once stress has abated. Plays an important role in protecting cells from severe heat shock and starvation, as well as in acid resistance of stationary-phase cells. It uses temperature-induced exposure of structured hydrophobic domains to capture and stabilizes early unfolding and denatured protein intermediates under severe thermal stress. Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. It can also use phenylglyoxal as substrate. Glyoxalase activity protects cells against dicarbonyl stress. Displays an aminopeptidase activity that is specific against peptide substrates with alanine or basic amino acids (lysine, arginine) at N-terminus.<ref>PMID:7848303</ref> <ref>PMID:12235139</ref> <ref>PMID:12565879</ref> <ref>PMID:14731284</ref> <ref>PMID:15550391</ref> <ref>PMID:16796689</ref> <ref>PMID:17158627</ref> <ref>PMID:21696459</ref> |
- | < | + | == 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/n5/1n57_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=1n57 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Baneyx F]] |
- | [[Category: | + | [[Category: Hol WGJ]] |
- | [[Category: | + | [[Category: Korotkov K]] |
- | [[Category: | + | [[Category: Quigley PM]] |
- | + |
Current revision
Crystal Structure of Chaperone Hsp31
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