1y4s

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(New page: 200px<br /><applet load="1y4s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y4s, resolution 2.9&Aring;" /> '''Conformation rearrang...)
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[[Image:1y4s.gif|left|200px]]<br /><applet load="1y4s" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1y4s, resolution 2.9&Aring;" />
 
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'''Conformation rearrangement of heat shock protein 90 upon ADP binding'''<br />
 
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==Overview==
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==Conformation rearrangement of heat shock protein 90 upon ADP binding==
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Hsp90 is an abundant molecular chaperone involved in many biological, systems. We report here the crystal structures of the unliganded and ADP, bound fragments containing the N-terminal and middle domains of HtpG, an, E. coli Hsp90. These domains are not connected through a flexible linker, as often portrayed in models, but are intimately associated with one, another. The individual HtpG domains have similar folding to those of DNA, gyrase B but assemble differently, suggesting somewhat different, mechanisms for the ATPase superfamily. ADP binds to a subpocket of a large, site that is jointly formed by the N-terminal and middle domains and, induces conformational changes of the N-terminal domain. We speculate that, this large pocket serves as a putative site for binding of client, proteins/cochaperones. Modeling shows that ATP is not exposed to the, molecular surface, thus implying that ATP activation of hsp90 chaperone, activities is accomplished via conformational changes.
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<StructureSection load='1y4s' size='340' side='right'caption='[[1y4s]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1y4s]] is a 2 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=1Y4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y4S 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]] 2.9&#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=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=1y4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y4s OCA], [https://pdbe.org/1y4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y4s RCSB], [https://www.ebi.ac.uk/pdbsum/1y4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y4s 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/y4/1y4s_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=1y4s 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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1Y4S 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 and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y4S 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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Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding., Huai Q, Wang H, Liu Y, Kim HY, Toft D, Ke H, Structure. 2005 Apr;13(4):579-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15837196 15837196]
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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: Huai, Q.]]
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[[Category: Huai Q]]
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[[Category: Ke, H.]]
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[[Category: Ke H]]
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[[Category: Kim, H.]]
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[[Category: Kim H]]
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[[Category: Liu, Y.]]
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[[Category: Liu Y]]
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[[Category: Toft, D.]]
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[[Category: Toft D]]
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[[Category: Wang, H.]]
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[[Category: Wang H]]
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[[Category: ADP]]
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[[Category: MG]]
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[[Category: atpase]]
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[[Category: hsp90]]
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[[Category: htpg]]
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[[Category: molecular chaperone]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:34:01 2007''
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Current revision

Conformation rearrangement of heat shock protein 90 upon ADP binding

PDB ID 1y4s

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