Water orientation and dynamics in the closed and open influenza B virus M2 proton channels
Name
s42003-021-01847-2.pdf
Description
Published version
Size
2.77 MB
Format
Unknown
Checksum (MD5)
a3880bb003755c1a9599a15154cd2240
Author(s)
Gelenter, Martin David
Mandala, Venkata Shiva
Niesen, Michiel JM
Sharon, Dina A
Dregni, Aurelio J
Willard, Adam P.
Hong, Mei
Date Issued
2021
Journal
Communications Biology
Publisher
Springer Science and Business Media LLC
Version
Final published version
Abstract
© 2021, The Author(s). The influenza B M2 protein forms a water-filled tetrameric channel to conduct protons across the lipid membrane. To understand how channel water mediates proton transport, we have investigated the water orientation and dynamics using solid-state NMR spectroscopy and molecular dynamics (MD) simulations. 13C-detected water 1H NMR relaxation times indicate that water has faster rotational motion in the low-pH open channel than in the high-pH closed channel. Despite this faster dynamics, the open-channel water shows higher orientational order, as manifested by larger motionally-averaged 1H chemical shift anisotropies. MD simulations indicate that this order is induced by the cationic proton-selective histidine at low pH. Furthermore, the water network has fewer hydrogen-bonding bottlenecks in the open state than in the closed state. Thus, faster dynamics and higher orientational order of water molecules in the open channel establish the water network structure that is necessary for proton hopping.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Creative Commons Attribution-NonCommercial-NoDerivs License
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1038/s42003-021-01847-2
