A proposed time-resolved X-ray scattering approach to track local and global conformational changes in membrane transport proteins

Structure
Magnus AnderssonRichard Neutze

Abstract

Time-resolved X-ray scattering has emerged as a powerful technique for studying the rapid structural dynamics of small molecules in solution. Membrane-protein-catalyzed transport processes frequently couple large-scale conformational changes of the transporter with local structural changes perturbing the uptake and release of the transported substrate. Using light-driven halide ion transport catalyzed by halorhodopsin as a model system, we combine molecular dynamics simulations with X-ray scattering calculations to demonstrate how small-molecule time-resolved X-ray scattering can be extended to the study of membrane transport processes. In particular, by introducing strongly scattering atoms to label specific positions within the protein and substrate, the technique of time-resolved wide-angle X-ray scattering can reveal both local and global conformational changes. This approach simultaneously enables the direct visualization of global rearrangements and substrate movement, crucial concepts that underpin the alternating access paradigm for membrane transport proteins.

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Citations

Feb 2, 2010·HFSP Journal·Alexandre SpechtMaurice Goeldner
Sep 29, 2011·Current Opinion in Structural Biology·Moran GrossmanIrit Sagi
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Jun 12, 2014·Biochimica Et Biophysica Acta·Cecilia WickstrandRichard Neutze
Sep 15, 2009·Structure·Magnus AnderssonRichard Neutze
Feb 19, 2010·Acta Crystallographica. Section A, Foundations of Crystallography·Sebastian WestenhoffRichard Neutze
Sep 8, 2016·Proceedings of the National Academy of Sciences of the United States of America·Levin U L Brinkmann, Jochen S Hub
Jul 16, 2008·Science·Federico Forneris, Andrea Mattevi
Mar 29, 2020·Science Advances·Harsha RavishankarMagnus Andersson
May 10, 2020·Journal of Synchrotron Radiation·Jungmin KimHyotcherl Ihee
Jan 8, 2021·The Journal of Membrane Biology·Fredrik Orädd, Magnus Andersson
Nov 18, 2021·Science Advances·Fredrik OräddMagnus Andersson

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