1n57

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[[Image:1n57.png|left|200px]]
 
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==Crystal Structure of Chaperone Hsp31==
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The line below this paragraph, containing "STRUCTURE_1n57", creates the "Structure Box" on the page.
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<StructureSection load='1n57' size='340' side='right'caption='[[1n57]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<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>
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{{STRUCTURE_1n57| PDB=1n57 | SCENE= }}
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<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>
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</table>
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===Crystal Structure of Chaperone Hsp31===
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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The line below this paragraph, {{ABSTRACT_PUBMED_12621151}}, adds the Publication Abstract to the page
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Check<jmol>
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(as it appears on PubMed at http://www.pubmed.gov), where 12621151 is the PubMed ID number.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n5/1n57_consurf.spt"</scriptWhenChecked>
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{{ABSTRACT_PUBMED_12621151}}
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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1N57 is a [[Single protein]] structure of sequence from [http://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].
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</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].
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<div style="clear:both"></div>
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==Reference==
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== References ==
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The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad., Quigley PM, Korotkov K, Baneyx F, Hol WG, Proc Natl Acad Sci U S A. 2003 Mar 18;100(6):3137-42. Epub 2003 Mar 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12621151 12621151]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Baneyx, F.]]
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[[Category: Baneyx F]]
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[[Category: Hol, W G.J.]]
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[[Category: Hol WGJ]]
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[[Category: Korotkov, K.]]
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[[Category: Korotkov K]]
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[[Category: Quigley, P M.]]
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[[Category: Quigley PM]]
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[[Category: Alpha-beta sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:34:13 2008''
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Current revision

Crystal Structure of Chaperone Hsp31

PDB ID 1n57

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