2ioq

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[[Image:2ioq.gif|left|200px]]<br /><applet load="2ioq" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ioq, resolution 3.50&Aring;" />
 
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'''Crystal Structure of full-length HTPG, the Escherichia coli HSP90'''<br />
 
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==Overview==
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==Crystal Structure of full-length HTPG, the Escherichia coli HSP90==
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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='2ioq' size='340' side='right'caption='[[2ioq]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2ioq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The December 2008 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Hsp90'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2008_12 10.2210/rcsb_pdb/mom_2008_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IOQ 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]] 3.5&#8491;</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=2ioq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ioq OCA], [https://pdbe.org/2ioq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ioq RCSB], [https://www.ebi.ac.uk/pdbsum/2ioq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ioq 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/2ioq_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=2ioq 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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2IOQ is a [http://en.wikipedia.org/wiki/Single_protein 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=2IOQ OCA].
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Hsp90]]
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[[Category: Agard, D A.]]
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[[Category: Large Structures]]
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[[Category: Harris, S F.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Shiau, A K.]]
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[[Category: Agard DA]]
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[[Category: chaperone]]
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[[Category: Harris SF]]
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[[Category: heat shock protein]]
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[[Category: Shiau AK]]
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[[Category: hsp90]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:54:40 2008''
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Current revision

Crystal Structure of full-length HTPG, the Escherichia coli HSP90

PDB ID 2ioq

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