2ior

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(New page: 200px<br /><applet load="2ior" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ior, resolution 1.65&Aring;" /> '''Crystal Structure of...)
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[[Image:2ior.gif|left|200px]]<br /><applet load="2ior" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ior, resolution 1.65&Aring;" />
 
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'''Crystal Structure of the N-terminal Domain of HtpG, the Escherichia coli Hsp90, Bound to ADP'''<br />
 
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==Overview==
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==Crystal Structure of the N-terminal Domain of HtpG, the Escherichia coli Hsp90, Bound to ADP==
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In eukaryotes, the ubiquitous and abundant members of the 90 kilodalton, heat-shock protein (hsp90) chaperone family facilitate the folding and, conformational changes of a broad array of proteins important in cell, signaling, proliferation, and survival. Here we describe the effects of, nucleotides on the structure of full-length HtpG, the Escherichia coli, hsp90 ortholog. By electron microscopy, the nucleotide-free, AMPPNP bound, and ADP bound states of HtpG adopt completely distinct conformations., Structural characterization of nucleotide-free and ADP bound HtpG was, extended to higher resolution by X-ray crystallography. In the absence of, nucleotide, HtpG exhibits an "open" conformation in which the three, domains of each monomer present hydrophobic elements into the large cleft, formed by the dimer. By contrast, ADP binding drives dramatic, conformational changes that allow these hydrophobic elements to converge, and shield each other from solvent, suggesting a mechanism by which, nucleotides could control client protein binding and release.
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<StructureSection load='2ior' size='340' side='right'caption='[[2ior]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2ior]] 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=2IOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IOR 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]] 1.65&#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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2ior FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ior OCA], [https://pdbe.org/2ior PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ior RCSB], [https://www.ebi.ac.uk/pdbsum/2ior PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ior ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HTPG_ECOLI HTPG_ECOLI] Molecular chaperone. Has ATPase activity.[HAMAP-Rule:MF_00505]
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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/io/2ior_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=2ior ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In eukaryotes, the ubiquitous and abundant members of the 90 kilodalton heat-shock protein (hsp90) chaperone family facilitate the folding and conformational changes of a broad array of proteins important in cell signaling, proliferation, and survival. Here we describe the effects of nucleotides on the structure of full-length HtpG, the Escherichia coli hsp90 ortholog. By electron microscopy, the nucleotide-free, AMPPNP bound, and ADP bound states of HtpG adopt completely distinct conformations. Structural characterization of nucleotide-free and ADP bound HtpG was extended to higher resolution by X-ray crystallography. In the absence of nucleotide, HtpG exhibits an "open" conformation in which the three domains of each monomer present hydrophobic elements into the large cleft formed by the dimer. By contrast, ADP binding drives dramatic conformational changes that allow these hydrophobic elements to converge and shield each other from solvent, suggesting a mechanism by which nucleotides could control client protein binding and release.
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==About this Structure==
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Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements.,Shiau AK, Harris SF, Southworth DR, Agard DA Cell. 2006 Oct 20;127(2):329-40. PMID:17055434<ref>PMID:17055434</ref>
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2IOR 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 MG, ADP and HEZ as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IOR OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements., Shiau AK, Harris SF, Southworth DR, Agard DA, Cell. 2006 Oct 20;127(2):329-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17055434 17055434]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 2ior" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Agard, D.A.]]
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[[Category: Harris, S.F.]]
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[[Category: Shiau, A.K.]]
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[[Category: ADP]]
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[[Category: HEZ]]
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[[Category: MG]]
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[[Category: chaperone]]
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[[Category: heat shock protein]]
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[[Category: hsp90]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:24:31 2007''
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Agard DA]]
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[[Category: Harris SF]]
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[[Category: Shiau AK]]

Current revision

Crystal Structure of the N-terminal Domain of HtpG, the Escherichia coli Hsp90, Bound to ADP

PDB ID 2ior

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