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1hw7

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[[Image:1hw7.jpg|left|200px]]
 
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==HSP33, HEAT SHOCK PROTEIN WITH REDOX-REGULATED CHAPERONE ACTIVITY==
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The line below this paragraph, containing "STRUCTURE_1hw7", creates the "Structure Box" on the page.
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<StructureSection load='1hw7' size='340' side='right'caption='[[1hw7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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'>[[1hw7]] 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=1HW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HW7 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1hw7| PDB=1hw7 | 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=1hw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hw7 OCA], [https://pdbe.org/1hw7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hw7 RCSB], [https://www.ebi.ac.uk/pdbsum/1hw7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hw7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HSLO_ECOLI HSLO_ECOLI] Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.[HAMAP-Rule:MF_00117]
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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/hw/1hw7_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=1hw7 ConSurf].
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<div style="clear:both"></div>
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'''HSP33, HEAT SHOCK PROTEIN WITH REDOX-REGULATED CHAPERONE ACTIVITY'''
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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__TOC__
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==Overview==
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</StructureSection>
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BACKGROUND: One strategy that cells employ to respond to environmental stresses (temperature, oxidation, and pathogens) is to increase the expression of heat shock proteins necessary to maintain viability. Several heat shock proteins function as molecular chaperones by binding unfolded polypeptides and preventing their irreversible aggregation. Hsp33, a highly conserved bacterial heat shock protein, is a redox-regulated molecular chaperone that appears to protect cells against the lethal effects of oxidative stress. RESULTS: The 2.2 A crystal structure of a truncated E. coli Hsp33 (residues 1-255) reveals a domain-swapped dimer. The core domain of each monomer (1-178) folds with a central helix that is sandwiched between two beta sheets. The carboxyl-terminal region (179-235), which lacks the intact Zn binding domain of Hsp33, folds into three helices that pack on the other subunit. The interface between the two core domains is comprised of conserved residues, including a rare Glu-Glu hydrogen bond across the dyad axis. Two potential polypeptide binding sites that span the dimer are observed: a long groove containing pockets of conserved and hydrophobic residues, and an intersubunit 10-stranded beta sheet "saddle" with a largely uncharged or hydrophobic surface. CONCLUSIONS: Hsp33 is a dimer in the crystal structure. Solution studies confirmed that this dimer reflects the structural changes that occur upon activation of Hsp33 as a molecular chaperone. Patterns of conserved residues and surface charges suggest that two grooves might be potential binding sites for protein folding intermediates.
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==About this Structure==
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1HW7 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=1HW7 OCA].
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==Reference==
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The 2.2 A crystal structure of Hsp33: a heat shock protein with redox-regulated chaperone activity., Vijayalakshmi J, Mukhergee MK, Graumann J, Jakob U, Saper MA, Structure. 2001 May 9;9(5):367-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11377197 11377197]
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[[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: Graumann, J.]]
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[[Category: Graumann J]]
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[[Category: Jakob, U.]]
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[[Category: Jakob U]]
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[[Category: Mukhergee, M K.]]
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[[Category: Mukhergee MK]]
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[[Category: Saper, M A.]]
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[[Category: Saper MA]]
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[[Category: Vijayalakshmi, J.]]
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[[Category: Vijayalakshmi J]]
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[[Category: Crystal structure]]
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[[Category: Dimerization]]
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[[Category: Heat shock protein]]
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[[Category: Hsp33]]
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[[Category: Oxidative stress]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:17:35 2008''
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Current revision

HSP33, HEAT SHOCK PROTEIN WITH REDOX-REGULATED CHAPERONE ACTIVITY

PDB ID 1hw7

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