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1i7f

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[[Image:1i7f.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF THE HSP33 DOMAIN WITH CONSTITUTIVE CHAPERONE ACTIVITY==
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|PDB= 1i7f |SIZE=350|CAPTION= <scene name='initialview01'>1i7f</scene>, resolution 2.7&Aring;
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<StructureSection load='1i7f' size='340' side='right'caption='[[1i7f]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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<table><tr><td colspan='2'>[[1i7f]] 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=1I7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I7F FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.7&#8491;</td></tr>
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|GENE= HSP33 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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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=1i7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i7f OCA], [https://pdbe.org/1i7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i7f RCSB], [https://www.ebi.ac.uk/pdbsum/1i7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i7f 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/i7/1i7f_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=1i7f ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF THE HSP33 DOMAIN WITH CONSTITUTIVE 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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Heat shock protein 33 (Hsp33) inhibits aggregation of partially denatured proteins during oxidative stress. The chaperone activity of Hsp33 is unique among heat shock proteins because the activity is reversibly regulated by cellular redox status. We report here the crystal structure of the N-terminal region of Hsp33 fragments with constitutive chaperone activity. The structure reveals that the N-terminal portion of Hsp33 forms a tightly associated dimer formed by a domain crossover. A concave groove on the dimeric surface contains an elongated hydrophobic patch that could potentially bind denatured protein substrates. The termini of the subunits are located near the hydrophobic patch, indicating that the cleaved C-terminal domain may shield the hydrophobic patch in an inactive state. Two of the four conserved zinc-coordinating cysteines are in the end of the N-terminal domain, and the other two are in the cleaved C-terminal domain. The structural information and subsequent biochemical characterizations suggest that the redox switch of Hsp33 occurs by a reversible dissociation of the C-terminal regulatory domain through oxidation of zinc-coordinating cysteines and zinc release.
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==About this Structure==
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1I7F 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=1I7F OCA].
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==Reference==
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Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity., Kim SJ, Jeong DG, Chi SW, Lee JS, Ryu SE, Nat Struct Biol. 2001 May;8(5):459-66. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11323724 11323724]
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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: Chi, S W.]]
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[[Category: Chi S-W]]
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[[Category: Jeong, D G.]]
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[[Category: Jeong D-G]]
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[[Category: Kim, S J.]]
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[[Category: Kim S-J]]
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[[Category: Lee, J S.]]
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[[Category: Lee J-S]]
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[[Category: Ryu, S E.]]
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[[Category: Ryu S-E]]
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[[Category: GOL]]
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[[Category: SO4]]
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[[Category: hsp33]]
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[[Category: redox sensitive molecular chaperone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:46:29 2008''
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Current revision

CRYSTAL STRUCTURE OF THE HSP33 DOMAIN WITH CONSTITUTIVE CHAPERONE ACTIVITY

PDB ID 1i7f

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