2ior

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[[Image:2ior.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of the N-terminal Domain of HtpG, the Escherichia coli Hsp90, Bound to ADP==
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|PDB= 2ior |SIZE=350|CAPTION= <scene name='initialview01'>2ior</scene>, resolution 1.65&Aring;
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<StructureSection load='2ior' size='340' side='right'caption='[[2ior]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>
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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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|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]] 1.65&#8491;</td></tr>
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|GENE= htpG ([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=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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}}
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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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'''Crystal Structure of the N-terminal Domain of HtpG, the Escherichia coli Hsp90, Bound to ADP'''
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ior" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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== References ==
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==About this Structure==
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<references/>
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2IOR 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=2IOR OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/17055434 17055434]
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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: Agard, D A.]]
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[[Category: Agard DA]]
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[[Category: Harris, S F.]]
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[[Category: Harris SF]]
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[[Category: Shiau, A K.]]
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[[Category: Shiau AK]]
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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://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:32:00 2008''
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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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OCA

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