1usv: Difference between revisions
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[[Image:1usv.jpg|left|200px]] | [[Image:1usv.jpg|left|200px]] | ||
'''THE STRUCTURE OF THE COMPLEX BETWEEN AHA1 AND HSP90''' | {{Structure | ||
|PDB= 1usv |SIZE=350|CAPTION= <scene name='initialview01'>1usv</scene>, resolution 2.70Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
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'''THE STRUCTURE OF THE COMPLEX BETWEEN AHA1 AND HSP90''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1USV is a [ | 1USV is a [[Protein complex]] structure of sequences 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=1USV OCA]. | ||
==Reference== | ==Reference== | ||
Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery., Meyer P, Prodromou C, Liao C, Hu B, Roe SM, Vaughan CK, Vlasic I, Panaretou B, Piper PW, Pearl LH, EMBO J. 2004 Mar 24;23(6):1402-10. PMID:[http:// | Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery., Meyer P, Prodromou C, Liao C, Hu B, Roe SM, Vaughan CK, Vlasic I, Panaretou B, Piper PW, Pearl LH, EMBO J. 2004 Mar 24;23(6):1402-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15039704 15039704] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: hsp90]] | [[Category: hsp90]] | ||
''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 14:36:27 2008'' | ||
Revision as of 15:36, 20 March 2008
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THE STRUCTURE OF THE COMPLEX BETWEEN AHA1 AND HSP90
OverviewOverview
Hsp90 is a molecular chaperone essential for the activation and assembly of many key eukaryotic signalling and regulatory proteins. Hsp90 is assisted and regulated by co-chaperones that participate in an ordered series of dynamic multiprotein complexes, linked to Hsp90 conformationally coupled ATPase cycle. The co-chaperones Aha1 and Hch1 bind to Hsp90 and stimulate its ATPase activity. Biochemical analysis shows that this activity is dependent on the N-terminal domain of Aha1, which interacts with the central segment of Hsp90. The structural basis for this interaction is revealed by the crystal structure of the N-terminal domain (1-153) of Aha1 (equivalent to the whole of Hch1) in complex with the middle segment of Hsp90 (273-530). Structural analysis and mutagenesis show that binding of N-Aha1 promotes a conformational switch in the middle-segment catalytic loop (370-390) of Hsp90 that releases the catalytic Arg 380 and enables its interaction with ATP in the N-terminal nucleotide-binding domain of the chaperone.
About this StructureAbout this Structure
1USV is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery., Meyer P, Prodromou C, Liao C, Hu B, Roe SM, Vaughan CK, Vlasic I, Panaretou B, Piper PW, Pearl LH, EMBO J. 2004 Mar 24;23(6):1402-10. PMID:15039704
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