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1byq

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[[Image:1byq.gif|left|200px]]
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{{STRUCTURE_1byq| PDB=1byq | SCENE= }}
{{STRUCTURE_1byq| PDB=1byq | SCENE= }}
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'''HSP90 N-TERMINAL DOMAIN BOUND TO ADP-MG'''
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===HSP90 N-TERMINAL DOMAIN BOUND TO ADP-MG===
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==Overview==
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Heat shock protein 90 (Hsp90), an abundant molecular chaperone in the eukaryotic cytosol, is involved in the folding of a set of cell regulatory proteins and in the re-folding of stress-denatured polypeptides. The basic mechanism of action of Hsp90 is not yet understood. In particular, it has been debated whether Hsp90 function is ATP dependent. A recent crystal structure of the NH2-terminal domain of yeast Hsp90 established the presence of a conserved nucleotide binding site that is identical with the binding site of geldanamycin, a specific inhibitor of Hsp90. The functional significance of nucleotide binding by Hsp90 has remained unclear. Here we present evidence for a slow but clearly detectable ATPase activity in purified Hsp90. Based on a new crystal structure of the NH2-terminal domain of human Hsp90 with bound ADP-Mg and on the structural homology of this domain with the ATPase domain of Escherichia coli DNA gyrase, the residues of Hsp90 critical in ATP binding (D93) and ATP hydrolysis (E47) were identified. The corresponding mutations were made in the yeast Hsp90 homologue, Hsp82, and tested for their ability to functionally replace wild-type Hsp82. Our results show that both ATP binding and hydrolysis are required for Hsp82 function in vivo. The mutant Hsp90 proteins tested are defective in the binding and ATP hydrolysis-dependent cycling of the co-chaperone p23, which is thought to regulate the binding and release of substrate polypeptide from Hsp90. Remarkably, the complete Hsp90 protein is required for ATPase activity and for the interaction with p23, suggesting an intricate allosteric communication between the domains of the Hsp90 dimer. Our results establish Hsp90 as an ATP-dependent chaperone.
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(as it appears on PubMed at http://www.pubmed.gov), where 9817749 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9817749}}
==About this Structure==
==About this Structure==
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[[Category: Atp binding]]
[[Category: Atp binding]]
[[Category: Chaperone protein]]
[[Category: Chaperone protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:07:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:57:49 2008''

Revision as of 16:57, 30 June 2008

Image:1byq.png

Template:STRUCTURE 1byq

HSP90 N-TERMINAL DOMAIN BOUND TO ADP-MG

Template:ABSTRACT PUBMED 9817749

About this Structure

1BYQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis., Obermann WM, Sondermann H, Russo AA, Pavletich NP, Hartl FU, J Cell Biol. 1998 Nov 16;143(4):901-10. PMID:9817749

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