Oligomeric Structure of Anabaena Sensory Rhodopsin in a Lipid Bilayer Environment by Combining Solid-State NMR and Long-range DEER Constraints

Journal of Molecular Biology
Sergey MilikisiyantsAlex I Smirnov

Abstract

Oligomerization of membrane proteins is common in nature. Here, we combine spin-labeling double electron-electron resonance (DEER) and solid-state NMR (ssNMR) spectroscopy to refine the structure of an oligomeric integral membrane protein, Anabaena sensory rhodopsin (ASR), reconstituted in a lipid environment. An essential feature of such a combined approach is that it provides structural distance restraints spanning a range of ca 3-60Å while using the same sample preparation (i.e., mutations, paramagnetic labeling, and reconstitution in lipid bilayers) for both ssNMR and DEER. Direct modeling of the multispin effects on DEER signal allowed for the determination of the oligomeric order and for obtaining long-range DEER distance restraints between the ASR trimer subunits that were used to refine the ssNMR structure of ASR. The improved structure of the ASR trimer revealed a more compact packing of helices and side chains at the intermonomer interface, compared to the structure determined using the ssNMR data alone. The extent of the refinement is significant when compared with typical helix movements observed for the active states of homologous proteins. Our combined approach of using complementary DEER and NMR measurements for ...Continue Reading

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Citations

Feb 9, 2019·Physical Chemistry Chemical Physics : PCCP·Austin Gamble JarviSunil Saxena
May 18, 2020·Biomolecules·Indra D Sahu, Gary A Lorigan
Aug 29, 2019·Nature Communications·Peng XiaoVladimir Ladizhansky
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Apr 20, 2018·Emerging Topics in Life Sciences·Gunnar Jeschke
May 14, 2021·The Journal of Physical Chemistry. B·Zikri HasanbasriSunil Saxena
Oct 28, 2019·Journal of Chemical Theory and Computation·Malte SiemersAna-Nicoleta Bondar
Mar 30, 2019·The Journal of Physical Chemistry. B·Matthew N IdsoSongi Han

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