1y4u: Difference between revisions

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<StructureSection load='1y4u' size='340' side='right'caption='[[1y4u]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='1y4u' size='340' side='right'caption='[[1y4u]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1y4u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1Y4U FirstGlance]. <br>
<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1y4s|1y4s]]</div></td></tr>
</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">htpG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1y4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y4u OCA], [http://pdbe.org/1y4u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y4u RCSB], [http://www.ebi.ac.uk/pdbsum/1y4u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y4u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HTPG_ECOLI HTPG_ECOLI]] Molecular chaperone. Has ATPase activity.[HAMAP-Rule:MF_00505]  
[https://www.uniprot.org/uniprot/HTPG_ECOLI HTPG_ECOLI] Molecular chaperone. Has ATPase activity.[HAMAP-Rule:MF_00505]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1y4u ConSurf].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:15837196<ref>PMID:15837196</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1y4u" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[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: Chaperone]]
[[Category: Hsp90]]
[[Category: Htpg]]
[[Category: Molecular chaperone]]
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