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Dynamics of Bacteriorhodopsin in the Dark‐Adapted State from Solution NMR


Kooijman, Laurens; Schuster, Matthias; Baumann, Christian; Jurt, Simon; Löhr, Frank; Fürtig, Boris; Güntert, Peter; Zerbe, Oliver (2020). Dynamics of Bacteriorhodopsin in the Dark‐Adapted State from Solution NMR. Angewandte Chemie Internationale Edition:anie.202004393.

Abstract

To achieve efficient proton pumping in the light-driven proton pump bacteriorhodopsin, the protein must be tightly coupled to the retinal to rapidly convert retinal isomerization into protein structural rearrangements. Methyl group dynamics of bR embedded in lipid nanodiscs were determined in the dark-adapted state, and were found to be mostly well-ordered at the cytosolic side. Methyl groups in the M145A mutant of bR, which displays only 10% residual proton pumping activity, are less well ordered suggesting a link between side chain dynamics on the cytosolic side of the bR cavity and proton pumping activity. In addition, slow conformational exchange, attributed to low frequency motions of aromatic rings, was indirectly observed for residues on the extracellular side of the bR cavity. This may be related to reorganization of the water network. These observations provide a detailed picture of previously undescribed equilibrium dynamics on different time scales for ground-state bR.

Abstract

To achieve efficient proton pumping in the light-driven proton pump bacteriorhodopsin, the protein must be tightly coupled to the retinal to rapidly convert retinal isomerization into protein structural rearrangements. Methyl group dynamics of bR embedded in lipid nanodiscs were determined in the dark-adapted state, and were found to be mostly well-ordered at the cytosolic side. Methyl groups in the M145A mutant of bR, which displays only 10% residual proton pumping activity, are less well ordered suggesting a link between side chain dynamics on the cytosolic side of the bR cavity and proton pumping activity. In addition, slow conformational exchange, attributed to low frequency motions of aromatic rings, was indirectly observed for residues on the extracellular side of the bR cavity. This may be related to reorganization of the water network. These observations provide a detailed picture of previously undescribed equilibrium dynamics on different time scales for ground-state bR.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Uncontrolled Keywords:membrane proteins, GPCRs, protein dynamics
Language:English
Date:29 July 2020
Deposited On:30 Jul 2020 14:49
Last Modified:30 Jul 2020 14:50
Publisher:Wiley-VCH Verlag
ISSN:1433-7851
OA Status:Closed
Publisher DOI:https://doi.org/10.1002/anie.202004393
Project Information:
  • : FunderSNSF
  • : Grant ID310030_179314
  • : Project TitleTowards NMR studies of entire GPCRs
  • : FunderForschungskredit der Universität Zürich
  • : Grant IDFK- 18-083
  • : Project Title

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Language: English
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Embargo till: 2021-07-29