1y4u
From Proteopedia
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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
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
Page seeded by OCA on Wed Nov 21 06:34:05 2007
Categories: Escherichia coli | Single protein | Huai, Q. | Ke, H. | Kim, H. | Liu, Y. | Toft, D. | Wang, H. | Atpase | Hsp90 | Htpg | Molecular chaperone
