1y4u: Difference between revisions

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[[Image:1y4u.gif|left|200px]]
{{Seed}}
[[Image:1y4u.png|left|200px]]


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{{STRUCTURE_1y4u|  PDB=1y4u  |  SCENE=  }}  
{{STRUCTURE_1y4u|  PDB=1y4u  |  SCENE=  }}  


'''Conformation rearrangement of heat shock protein 90 upon ADP binding'''
===Conformation rearrangement of heat shock protein 90 upon ADP binding===




==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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{{ABSTRACT_PUBMED_15837196}}


==About this Structure==
==About this Structure==
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[[Category: Htpg]]
[[Category: Htpg]]
[[Category: Molecular chaperone]]
[[Category: Molecular chaperone]]
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Revision as of 10:02, 29 July 2008

File:1y4u.png

Template:STRUCTURE 1y4u

Conformation rearrangement of heat shock protein 90 upon ADP binding

Template:ABSTRACT PUBMED 15837196

About this Structure

1Y4U is a Single protein structure of sequence from Escherichia coli. 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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