Water orientation and dynamics in the closed and open influenza B virus M2 proton channels.

ABSTRACT: 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

SUBMITTER: Gelenter MD 

PROVIDER: S-EPMC7955094 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature