1hk7: Difference between revisions
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==Overview== | ==Overview== | ||
Activation of client proteins by the Hsp90 molecular chaperone is, dependent on binding and hydrolysis of ATP, which drives a molecular clamp, via transient dimerization of the N-terminal domains. The crystal, structure of the middle segment of yeast Hsp90 reveals considerable, evolutionary divergence from the equivalent regions of other GHKL protein, family members such as MutL and GyrB, including an additional domain of, new fold. Using the known structure of the N-terminal nucleotide binding, domain, a model for the Hsp90 dimer has been constructed. From this, structure, residues implicated in the ATPase-coupled conformational cycle, and in interactions with client proteins and the activating cochaperone, Aha1 have been identified, and their roles functionally characterized in, vitro . | Activation of client proteins by the Hsp90 molecular chaperone is, dependent on binding and hydrolysis of ATP, which drives a molecular clamp, via transient dimerization of the N-terminal domains. The crystal, structure of the middle segment of yeast Hsp90 reveals considerable, evolutionary divergence from the equivalent regions of other GHKL protein, family members such as MutL and GyrB, including an additional domain of, new fold. Using the known structure of the N-terminal nucleotide binding, domain, a model for the Hsp90 dimer has been constructed. From this, structure, residues implicated in the ATPase-coupled conformational cycle, and in interactions with client proteins and the activating cochaperone, Aha1 have been identified, and their roles functionally characterized in, vitro and in vivo. | ||
==About this Structure== | ==About this Structure== | ||
1HK7 is a | 1HK7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with CD and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HK7 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: heat shock protein]] | [[Category: heat shock protein]] | ||
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Revision as of 13:41, 5 November 2007
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MIDDLE DOMAIN OF HSP90
OverviewOverview
Activation of client proteins by the Hsp90 molecular chaperone is, dependent on binding and hydrolysis of ATP, which drives a molecular clamp, via transient dimerization of the N-terminal domains. The crystal, structure of the middle segment of yeast Hsp90 reveals considerable, evolutionary divergence from the equivalent regions of other GHKL protein, family members such as MutL and GyrB, including an additional domain of, new fold. Using the known structure of the N-terminal nucleotide binding, domain, a model for the Hsp90 dimer has been constructed. From this, structure, residues implicated in the ATPase-coupled conformational cycle, and in interactions with client proteins and the activating cochaperone, Aha1 have been identified, and their roles functionally characterized in, vitro and in vivo.
About this StructureAbout this Structure
1HK7 is a Single protein structure of sequence from Saccharomyces cerevisiae with CD and MG as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions., Meyer P, Prodromou C, Hu B, Vaughan C, Roe SM, Panaretou B, Piper PW, Pearl LH, Mol Cell. 2003 Mar;11(3):647-58. PMID:12667448
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