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Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane α-helical protein
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Good, Daryl B., Pham, Charlie, Jagas, Jacob, Lewandowski, Józef R. and Ladizhansky, Vladimir (2017) Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane α-helical protein. Journal of the American Chemical Society, 139 (27). pp. 9246-9258. doi:10.1021/jacs.7b03974 ISSN 0002-7863.
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Official URL: https://doi.org/10.1021/jacs.7b03974
Abstract
Proteins are dynamic entities and populate ensembles of conformations. Transitions between states within a conformational ensemble occur over a broad spectrum of amplitude and time scales, and are often related to biological function. Whereas solid-state NMR (SSNMR) spectroscopy has recently been used to characterize conformational ensembles of proteins in the microcrystalline states, its applications to membrane proteins remain limited. Here we use SSNMR to study conformational dynamics of a seven-helical transmembrane (TM) protein, Anabaena Sensory Rhodopsin (ASR) reconstituted in lipids. We report on site-specific measurements of the 15N longitudinal R1 and rotating frame R1ρ relaxation rates at two fields of 600 and 800 MHz and at two temperatures of 7 and 30°C. Quantitative analysis of the R1 and R1ρ values and of their field and temperature dependencies provides evidence of motions on at least two time scales. We modeled these motions as fast local motions and slower collective motions of TM helices and of structured loops, and used the simple model-free and extended model-free analyses to fit the data and estimate the amplitudes,
time scales and activation energies. Faster picosecond (tens to hundreds of picoseconds) local motions occur throughout the protein and are dominant in the middle portions of the TM helices. In contrast, the amplitudes of the slower collective motions occurring on the nanosecond (tens to hundreds of nanoseconds) time scales, are smaller in the central parts of helices, but increase toward their cytoplasmic sides as well as in the interhelical loops. ASR interacts with a soluble transducer protein on its cytoplasmic surface, and its binding affinity is modulated by light. The larger amplitude of motions on the cytoplasmic side of the TM helices correlates with the ability of ASR to undergo large conformational changes in the process of binding/unbinding the transducer.
Item Type: | Journal Article | ||||||||
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Subjects: | Q Science > QP Physiology | ||||||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||||||
Library of Congress Subject Headings (LCSH): | Membrane proteins, Nuclear magnetic resonance | ||||||||
Journal or Publication Title: | Journal of the American Chemical Society | ||||||||
Publisher: | American Chemical Society | ||||||||
ISSN: | 0002-7863 | ||||||||
Official Date: | 12 July 2017 | ||||||||
Dates: |
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Volume: | 139 | ||||||||
Number: | 27 | ||||||||
Page Range: | pp. 9246-9258 | ||||||||
DOI: | 10.1021/jacs.7b03974 | ||||||||
Status: | Peer Reviewed | ||||||||
Publication Status: | Published | ||||||||
Access rights to Published version: | Open Access (Creative Commons) | ||||||||
Date of first compliant deposit: | 3 July 2017 | ||||||||
Date of first compliant Open Access: | 18 January 2019 | ||||||||
Funder: | Natural Sciences and Engineering Research Council of Canada (NSERC), Canada Foundation for Innovation (CFI), Ontario. Ministry of Research and Innovation, Seventh Framework Programme (European Commission) (FP7), European Research Council (ERC), Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Bill & Melinda Gates Foundation | ||||||||
Grant number: | Discovery Grant RGPIN-2014-04547 (NSERC), (FP/2007-2013)/ERC Grant Agreement 639907 (FP7) (ERC), Grant BB/L022761/1 (BBSRC), OPP1160394 (Bill & Melinda Gates Foundation) | ||||||||
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