Kinetic response of a photoperturbed allosteric protein

TitleKinetic response of a photoperturbed allosteric protein
Publication TypeJournal Article
Year of Publication2013
AuthorsBuchli B., Waldauer S.A, Walser R., Donten M.L, Pfister R., Blöchliger N., Steiner S., Caflisch A., Zerbe O., Hamm P.
JournalProceedings of the National Academy of Sciences of the United States of America
Date Published2013 Jul 16
Type of ArticleResearch Article
KeywordsAllosteric 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

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.



Alternate JournalProc. Natl. Acad. Sci. U.S.A.
PubMed ID23818626
PubMed Central IDPMC3718176
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