1y4s

<table><tr><td colspan='2'>[[1y4s]] 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=1Y4S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Y4S FirstGlance]. <br>

</td></tr><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>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1y4u|1y4u]]</div></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'>[http://proteopedia.org/fgij/fg.htm?mol=1y4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y4s OCA], [http://pdbe.org/1y4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y4s RCSB], [http://www.ebi.ac.uk/pdbsum/1y4s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y4s ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/HTPG_ECOLI HTPG_ECOLI]] Molecular chaperone. Has ATPase activity.[HAMAP-Rule:MF_00505]

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== 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>

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<div class="pdbe-citations 1y4s" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Huai, Q]]

[[Category: Ke, H]]

[[Category: Kim, H]]

[[Category: Liu, Y]]

[[Category: Toft, D]]

[[Category: Wang, H]]

[[Category: Molecular chaperone]]