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The allosteric mechanism of the chaperonin GroEL: A dynamic analysis
Open accessAbstract
Normal mode calculations on individual subunits and a multisubunit construct are used to analyze the structural transitions that occur during the GroEL cycle. The normal modes demonstrate that the specific displacements of the domains (hinge bending, twisting) observed in the structural studies arise from the intrinsic flexibility of the subunits. The allosteric mechanism (positive cooperativity within a ring, negative cooperativity between rings) is shown to be based on coupled tertiary structural changes, rather than the quaternary transition found in classic allosteric proteins. The results unify static structural data from x-ray crystallography and cryoelectron microscopy with functional measurements of binding and cooperativity.
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Cited by
A Unified View of “How Allostery Works”
Tsai, C.-J., & Nussinov, R. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003394 · Cited by 401
Yang, L.-W., & Bahar, I. (2005) · Structure · doi:10.1016/j.str.2005.03.015 · Cited by 273
Controlling Allosteric Networks in Proteins
Dokholyan, N. V. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00544 · Cited by 260
Chennubhotla, C., Yang, Z., & Bahar, I. (2008) · Molecular BioSystems · doi:10.1039/b717819k · Cited by 102
Metadata
- Authors
- Ma, J., & Karplus, M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-07-21
- Volume
- 95
- Issue
- 15
- Pages
- 8502-8507
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2007832948
- Cited by
- 184
- References
- 0
- FWCI
- 2.03
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: The allosteric mechanism of the chaperonin GroEL: A dynamic analysis. https://app.cochat.ai/papers/10.1073/pnas.95.15.8502
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- Ma, J., & Karplus, M. (1998). The allosteric mechanism of the chaperonin GroEL: A dynamic analysis. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.15.8502
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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