Structural and Functional Analysis of the Middle Segment of Hsp90: Implications for ATP Hydrolysis and Client Protein and Cochaperone Interactions

Meyer, Philippe; Prodromou, Chrisostomos; Hu, Bin; Vaughan, Cara; Roe, S. Mark; Panaretou, Barry; Piper, Peter W.; Pearl, Laurence H.

doi:10.1016/s1097-2765(03)00065-0

Cited by 499Heat shock proteins researchProtein Structure and DynamicsUbiquitin and proteasome pathways

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Structural and Functional Analysis of the Middle Segment of Hsp90: Implications for ATP Hydrolysis and Client Protein and Cochaperone Interactions

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Meyer, Philippe, Prodromou, Chrisostomos, Hu, Bin, Vaughan, Cara, Roe, S. Mark, Panaretou, Barry, Piper, Peter W., Pearl, Laurence H.·2003·Molecular Cell

DOI 10.1016/s1097-2765(03)00065-0

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Abstract

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.

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Hsp90 W320 and F349 also contact GR in the loading complex, and Hsp90 W320 is critical for client activation in vivo.
“Notably, Hsp90W320,F349 also make contact with GR in the loading complex12 and Hsp90W320 is critical for client activation in vivo20-22.”
From Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism (2022) · cites this paper as [20]
The Client Protein Binding Sites section (p. 8) reports that a yeast Hsp90 Trp300Ala mutant had severe defects in growth and in vivo v-Src activation, supporting the functional point. Our copy does not identify Trp300 as W320, so it does not directly establish the claim for the specifically numbered residue. The GR-loading-complex contact is attached to a different citation in the citing sentence. (LLM, conf=0.78)
Experimental — accuracy not yet measured
R32A and R380A mutations disrupt NTD-MD contacts.
“we selected previously characterized mutants that either disrupt [R32A (34) and R380A (35)] or stabilize [A107N (26)] NTD-MD contacts.”
From Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network (2021) · cites this paper as [35]
In the MD, globular proteins interact with the Src loop and the N terminus of helix Mα2.
“In the MD, globular proteins interact with the “Src loop” (35) and the N terminus of helix Mα2.”
From Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network (2021) · cites this paper as [35]

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Authors: Meyer, P., Prodromou, C., Hu, B., Vaughan, C., Roe, S. M., Panaretou, B., Piper, P. W., & Pearl, L. H.
Affiliations: Institute of Cancer Research (GB)
King's College London (GB)
University College London (GB)
Corresponding author: Pearl, Laurence H.
ORCID: Meyer, Philippe
Prodromou, Chrisostomos
Hu, Bin
Vaughan, Cara
Roe, S. Mark
Panaretou, Barry
Piper, Peter W.
Pearl, Laurence H.
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2003-03
Volume: 11
Issue: 3
Pages: 647-658
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/s1097-2765(03)00065-0
OpenAlex: W2108255072
Cited by: 491
References: 52
Citations by year: 2026: 11 · 2025: 25 · 2024: 14 · 2023: 13 · 2022: 22 · 2021: 14 · 2020: 29 · 2019: 26 · 2018: 18 · 2017: 10 · 2016: 23 · 2015: 21 · 2014: 30 · 2013: 32 · 2012: 26
FWCI: 10.02
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3791 d)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
Sussex Research Online (University of Sussex) (submittedVersion, cc-by-nc)
UCL Discovery (University College London) (submittedVersion)
Figshare (submittedVersion, cc-by-nc)
Research Portal (King's College London) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: HSP90, ATP hydrolysis, MutL, gyrB, protein dimerization, nucleotide-binding domain, conformational cycle, molecular clamp, crystal structure, protein-protein interaction
MeSH terms: MutL Proteins, Adenosine Triphosphatases, Adenosine Triphosphate, Amino Acid Sequence, Binding Sites, Cell Division, Dose-Response Relationship, Drug, Fungal Proteins, Hydrolysis, Models, Molecular, Molecular Sequence Data, Mutation, Phenotype, Protein Binding, Protein Conformation, Structure-Activity Relationship, Temperature, Oncogene Protein pp60(v-src), Protein Structure, Tertiary, Crystallography, X-Ray, HSP90 Heat-Shock Proteins, Dimerization, DNA Gyrase, Escherichia coli Proteins

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Structural and Functional Analysis of the Middle Segment of Hsp90: Implications for ATP Hydrolysis and Client Protein and Cochaperone Interactions

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