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="350" color="white" frame="true" align="right" spinBox="true"
caption="1y4s, resolution 2.9&Aring;" />
caption="1y4s, resolution 2.9&Aring;" />
'''Conformation rearrangement of heat shock protein 90 upon ADP binding'''<br />
'''Conformation rearrangement of heat shock protein 90 upon ADP binding'''<br />
==Overview==
==Overview==
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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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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.
==About this Structure==
==About this Structure==
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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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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 <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y4S OCA].
==Reference==
==Reference==
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[[Category: molecular chaperone]]
[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:49 2008''

Revision as of 14:01, 21 February 2008

Image:1y4s.gif

1y4s, resolution 2.9Å

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Conformation rearrangement of heat shock protein 90 upon ADP binding

Overview

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.

About this Structure

1Y4S is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

Reference

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

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