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1ons

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(New page: 200px<br /><applet load="1ons" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ons, resolution 2.2&Aring;" /> '''Crystal structure of ...)
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[[Image:1ons.jpg|left|200px]]<br /><applet load="1ons" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ons, resolution 2.2&Aring;" />
 
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'''Crystal structure of Escherichia coli heat shock protein YedU'''<br />
 
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==Overview==
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==Crystal structure of Escherichia coli heat shock protein YedU==
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The mRNA of Escherichia coli yedU gene is induced 31-fold upon heat shock., The 31-kD YedU protein, also calls Hsp31, is highly conserved in several, human pathogens and has chaperone activity. We solved the crystal, structure of YedU at 2.2 A resolution. YedU monomer has an, alpha/beta/alpha sandwich domain and a small alpha/beta domain. YedU is a, dimer in solution, and its crystal structure indicates that a significant, amount of surface area is buried upon dimerization. There is an extended, hydrophobic patch that crosses the dimer interface on the surface of the, protein. This hydrophobic patch is likely the substrate-binding site, responsible for the chaperone activity. The structure also reveals a, potential protease-like catalytic triad composed of Cys184, His185, and, Asp213, although no enzymatic activity could be identified. YedU, coordinates a metal ion using His85, His122, and Glu90. This, 2-His-1-carboxylate motif is present in carboxypeptidase A (a zinc, enzyme), and a number of dioxygenases and hydroxylases that utilize iron, as a cofactor, suggesting another potential function for YedU.
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<StructureSection load='1ons' size='340' side='right'caption='[[1ons]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ons]] 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=1ONS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ONS 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]] 2.2&#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=ZN:ZINC+ION'>ZN</scene></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=1ons FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ons OCA], [https://pdbe.org/1ons PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ons RCSB], [https://www.ebi.ac.uk/pdbsum/1ons PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ons ProSAT]</span></td></tr>
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</table>
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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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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/on/1ons_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=1ons ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1ONS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ONS OCA].
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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== References ==
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==Reference==
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<references/>
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The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites., Zhao Y, Liu D, Kaluarachchi WD, Bellamy HD, White MA, Fox RO, Protein Sci. 2003 Oct;12(10):2303-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14500888 14500888]
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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: Fox, R.O.]]
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[[Category: Fox RO]]
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[[Category: Zhao, Y.]]
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[[Category: Zhao Y]]
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[[Category: ZN]]
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[[Category: chaperone]]
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[[Category: heat shock protein]]
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[[Category: hsp31]]
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[[Category: protease]]
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[[Category: stress response]]
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[[Category: yedu]]
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[[Category: zinc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:02:55 2007''
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Current revision

Crystal structure of Escherichia coli heat shock protein YedU

PDB ID 1ons

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