1hk7
From Proteopedia
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| - | [[Image:1hk7.gif|left|200px]] | + | [[Image:1hk7.gif|left|200px]] |
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| - | '''MIDDLE DOMAIN OF HSP90''' | + | {{Structure |
| + | |PDB= 1hk7 |SIZE=350|CAPTION= <scene name='initialview01'>1hk7</scene>, resolution 2.50Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''MIDDLE DOMAIN OF HSP90''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HK7 is a [ | + | 1HK7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HK7 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12667448 12667448] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: heat shock protein]] | [[Category: heat shock protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:38:07 2008'' |
Revision as of 09:38, 20 March 2008
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| , resolution 2.50Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MIDDLE DOMAIN OF HSP90
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 and in vivo.
About this Structure
1HK7 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 11:38:07 2008
Categories: Saccharomyces cerevisiae | Single protein | Meyer, P. | Pearl, L H. | Prodromou, C. | Roe, S M. | CD | MG | Atpase | Chaperone | Heat shock protein
