1usv

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[[Image:1usv.jpg|left|200px]]
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[[Image:1usv.png|left|200px]]
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{{STRUCTURE_1usv| PDB=1usv | SCENE= }}
{{STRUCTURE_1usv| PDB=1usv | SCENE= }}
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'''THE STRUCTURE OF THE COMPLEX BETWEEN AHA1 AND HSP90'''
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===THE STRUCTURE OF THE COMPLEX BETWEEN AHA1 AND HSP90===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15039704 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15039704}}
==About this Structure==
==About this Structure==
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[[Category: Chaperone]]
[[Category: Chaperone]]
[[Category: Hsp90]]
[[Category: Hsp90]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:38:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:01:02 2008''

Revision as of 05:01, 29 July 2008

Template:STRUCTURE 1usv

THE STRUCTURE OF THE COMPLEX BETWEEN AHA1 AND HSP90

Template:ABSTRACT PUBMED 15039704

About this Structure

1USV is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

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:15039704

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