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New page: left|200px<br /><applet load="1y4u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y4u, resolution 2.9Å" /> '''Conformation rearrang...
 
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[[Image:1y4u.gif|left|200px]]<br /><applet load="1y4u" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1y4u, resolution 2.9&Aring;" />
'''Conformation rearrangement of heat shock protein 90 upon ADP binding'''<br />


==Overview==
==Conformation rearrangement of heat shock protein 90 upon ADP binding==
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.
<StructureSection load='1y4u' size='340' side='right'caption='[[1y4u]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1y4u]] 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=1Y4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y4U FirstGlance]. <br>
</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y4u OCA], [https://pdbe.org/1y4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y4u RCSB], [https://www.ebi.ac.uk/pdbsum/1y4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y4u ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HTPG_ECOLI HTPG_ECOLI] Molecular chaperone. Has ATPase activity.[HAMAP-Rule:MF_00505]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y4/1y4u_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1y4u ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1Y4U 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y4U OCA].
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Huai, Q.]]
[[Category: Huai Q]]
[[Category: Ke, H.]]
[[Category: Ke H]]
[[Category: Kim, H.]]
[[Category: Kim H]]
[[Category: Liu, Y.]]
[[Category: Liu Y]]
[[Category: Toft, D.]]
[[Category: Toft D]]
[[Category: Wang, H.]]
[[Category: Wang H]]
[[Category: atpase]]
[[Category: hsp90]]
[[Category: htpg]]
[[Category: molecular chaperone]]
 
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