Kinetic response of a photoperturbed allosteric protein
| Title | Kinetic response of a photoperturbed allosteric protein |
| Publication Type | Journal Article |
| Year of Publication | 2013 |
| Authors | Buchli B., Waldauer S.A, Walser R., Donten M.L, Pfister R., Blöchliger N., Steiner S., Caflisch A., Zerbe O., Hamm P. |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 110 |
| Issue | 29 |
| Pagination | 11725-11730 |
| Date Published | 2013 Jul 16 |
| Type of Article | Research Article |
| Keywords | Allosteric Regulation, Azo Compounds, Humans, Kinetics, Lasers, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Dynamics Simulation, Photochemistry, Protein Conformation, Protein Tyrosine Phosphatase, Non-Receptor Type 13, Spectrophotometry, Infrared, Time Factors, Water |
| Abstract | By covalently linking an azobenzene photoswitch across the binding groove of a PDZ domain, a conformational transition, similar to the one occurring upon ligand binding to the unmodified domain, can be initiated on a picosecond timescale by a laser pulse. The protein structures have been characterized in the two photoswitch states through NMR spectroscopy and the transition between them through ultrafast IR spectroscopy and molecular dynamics simulations. The binding groove opens on a 100-ns timescale in a highly nonexponential manner, and the molecular dynamics simulations suggest that the process is governed by the rearrangement of the water network on the protein surface. We propose this rearrangement of the water network to be another possible mechanism of allostery. |
| DOI | 10.1073/pnas.1306323110 |
| pubindex | 0174 |
| Alternate Journal | Proc. Natl. Acad. Sci. U.S.A. |
| PubMed ID | 23818626 |
| PubMed Central ID | PMC3718176 |
