Multiple Conformations of E. coli Hsp90 in Solution: Insights into the Conformational Dynamics of Hsp90
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Hsp90, an essential eukaryotic chaperone, depends upon its intrinsic ATPase activity for function. Crystal structures of the bacterial Hsp90 homolog, HtpG, and the yeast Hsp90 reveal large domain rearrangements between the nucleotide-free and the nucleotide-bound forms. We used small-angle X-ray scattering and recently developed molecular modeling methods to characterize the solution structure of HtpG and demonstrate how it differs from known Hsp90 conformations. In addition to this HtpG conformation, we demonstrate that under physiologically relevant conditions, multiple conformations coexist in equilibrium. In solution, nucleotide-free HtpG adopts a more extended conformation than observed in the crystal, and upon the addition of AMPPNP, HtpG is in equilibrium between this open state and a closed state that is in good agreement with the yeast AMPPNP crystal structure. These studies provide a unique view of Hsp90 conformational dynamics and provide a model for the role of nucleotide in effecting conformational change.
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Biophysical data indicate that apo-Hsp90 populates a dynamic ensemble of extended conformations in solution.
“Biophysical data indicate that apo-Hsp90 populates a dynamic ensemble of extended conformations in solution (11, 12).”
From Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network (2021) · cites this paper as [12]
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- Authors
- Krukenberg, K. A., Förster, F., Rice, L. M., Sali, A., & Agard, D. A.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of California, San Francisco (US)
- Corresponding author
- Agard, David A.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2008-05
- Volume
- 16
- Issue
- 5
- Pages
- 755-765
- ISSN
- 0969-2126 (ISSN-L)
- PMC
- PMC2600884
- OpenAlex
- W2131991936
- Cited by
- 160
- References
- 36
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 4 · 2023: 5 · 2022: 4 · 2021: 6 · 2020: 5 · 2019: 4 · 2018: 13 · 2017: 14 · 2016: 14 · 2015: 9 · 2014: 9 · 2013: 10 · 2012: 16
- FWCI
- 6.03
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Structure (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health
- National Eye Institute (PN2EY016525)
- National Center for Research Resources (P41RR001209)
- 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
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- HSP90, HtpG, Escherichia coli, molecular chaperones, conformational dynamics, solution structure, nucleotide binding, ATPase activity, AMP-PNP, domain rearrangement, conformational equilibrium, small-angle X-ray scattering
- MeSH terms
- Adenylyl Imidodiphosphate, Escherichia coli, Models, Molecular, Protein Conformation, Solutions, X-Ray Diffraction, Protein Structure, Tertiary, HSP90 Heat-Shock Proteins, Dimerization, Escherichia coli Proteins, Scattering, Small Angle
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