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1izy

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==Crystal structure of Hsp31==
==Crystal structure of Hsp31==
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<StructureSection load='1izy' size='340' side='right' caption='[[1izy]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='1izy' size='340' side='right'caption='[[1izy]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1izy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IZY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IZY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1izy]] is a 2 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=1IZY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IZY FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=X:2-DEOXY-N7-(8,9-DIHYDRO-9-HYDROXY-10-DEHYDROXY-AFLATOXIN)GUANOSINE+MONOPHOSPHATE'>X</scene></td></tr>
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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]] 2.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1izz|1izz]]</td></tr>
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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=1izy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1izy OCA], [https://pdbe.org/1izy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1izy RCSB], [https://www.ebi.ac.uk/pdbsum/1izy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1izy ProSAT]</span></td></tr>
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<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=1izy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1izy OCA], [http://pdbe.org/1izy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1izy RCSB], [http://www.ebi.ac.uk/pdbsum/1izy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1izy ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
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[[Category: Cha, S S]]
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[[Category: Large Structures]]
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[[Category: Lee, S J]]
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[[Category: Cha SS]]
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[[Category: Alpha-beta sandwitch]]
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[[Category: Lee SJ]]
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[[Category: Chaperone]]
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[[Category: Hydrolase]]
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Current revision

Crystal structure of Hsp31

PDB ID 1izy

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