1Y4U

Conformation rearrangement of heat shock protein 90 upon ADP binding

Summary for 1Y4U

• Entry DOI: 10.2210/pdb1y4u/pdb
• Related: 1y4s
• Descriptor: Chaperone protein htpG (1 entity in total)
• Functional Keywords: hsp90, htpg, molecular chaperone, atpase, chaperone
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A6Z3
• Total number of polymer chains: 2
• Total formula weight: 127921.49

Authors

Huai, Q.,Wang, H.,Liu, Y.,Kim, H.,Toft, D.,Ke, H. (deposition date: 2004-12-01, release date: 2005-04-19, Last modification date: 2024-04-03)

Primary citation

Huai, Q.,Wang, H.,Liu, Y.,Kim, H.Y.,Toft, D.,Ke, H.
Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding.
Structure, 13:579-590, 2005

PubMed Abstract: 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.

PubMed: 15837196
DOI: 10.1016/j.str.2004.12.018

Experimental method

X-RAY DIFFRACTION (2.9 Å)