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Anatomy of a Conformational Change: Hinged "Lid" Motion of the Triosephosphate Isomerase Loop
Abstract
Triosephosphate isomerase (TIM) is used as a model system for the study of how a localized conformational change in a protein structure is produced and related to enzyme reactivity. An 11-residue loop region moves more than 7 angstroms and closes over the active site when substrate binds. The loop acts like a "lid" in that it moves rigidly and is attached by two hinges to the remainder of the protein. The nature of the motion appears to be built into the loop by conserved residues; the hinge regions, in contrast, are not conserved. Results of molecular dynamics calculations confirm the structural analysis and suggest a possible ligand-induced mechanism for loop closure.
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Cited by
The Energy Landscapes and Motions of Proteins
Frauenfelder, H., Sligar, S. G., & Wolynes, P. G. (1991) · Science · doi:10.1126/science.1749933 · Cited by 3,250
Modeling of loops in protein structures
Fiser, A., Do, R. K. G., & Šali, A. (2000) · Protein Science · doi:10.1110/ps.9.9.1753 · Cited by 2,116
Enzyme catalysis: not different, just better
Knowles, J. R. (1991) · Nature · doi:10.1038/350121a0 · Cited by 567
Multiple diverse ligands binding at a single protein site: A matter of pre‐existing populations
Ma, B., Shatsky, M., Wolfson, H. J., & Nussinov, R. (2002) · Protein Science · doi:10.1110/ps.21302 · Cited by 420
Hoog, S. S., Pawlowski, J. E., Alzari, P. M., Penning, T. M., & Lewis, M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.7.2517 · Cited by 137
Metadata
- Authors
- Joseph, D., Petsko, G. A., & Karplus, M.
- Venue
- Science
- Published
- 1990-09-21
- Volume
- 249
- Issue
- 4975
- Pages
- 1425-1428
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2037612112
- Cited by
- 281
- References
- 0
- FWCI
- 6.75
- Type
- journal article
- Language
- en
- Open access
- closed
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- Joseph, D., Petsko, G. A., & Karplus, M. (1990). Anatomy of a Conformational Change: Hinged "Lid" Motion of the Triosephosphate Isomerase Loop. Science. https://doi.org/10.1126/science.2402636
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
