Mechanisms of Proton Conduction and Gating in Influenza M2 Proton Channels from Solid-State NMR

Author:

Hu Fanghao1,Luo Wenbin1,Hong Mei1

Affiliation:

1. Department of Chemistry, Iowa State University, Ames, IA 50011, USA.

Abstract

M2 Out of the Envelope The M2 protein from influenza A virus forms an acid-activated tetrameric proton channel in the viral envelope and is essential for viral replication. Two manuscripts shed light on the functional mechanism of this channel. Sharma et al. (p. 509 ; see the Perspective by Fiorin et al. ) determined the structure of the conductance domain in a lipid bilayer and propose that a histidine and tryptophan from each monomer form a cluster that guides protons through the channel in a mechanism that involves forming and breaking hydrogen bonds between adjacent pairs of histidines. Hu et al. (p. 505 ; see the Perspective by Fiorin et al. ) focused on the structure and dynamics of the proton-selective histidine at high and low pH, proposing that proton conduction involves histidine deprotonation and reprotonation.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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