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pH-induced conformational change of the influenza M2 protein C-terminal domain.
Nguyen PA
,
Soto CS
,
Polishchuk A
,
Caputo GA
,
Tatko CD
,
Ma C
,
Ohigashi Y
,
Pinto LH
,
DeGrado WF
,
Howard KP
.
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The M2 protein from influenza A is a pH-activated proton channel that plays an essential role in the viral life cycle and serves as a drug target. Using spin labeling EPR spectroscopy, we studied a 38-residue M2 peptide spanning the transmembrane region and its C-terminal extension. We obtained residue-specific environmental parameters under both high- and low-pH conditions for nine consecutive C-terminal sites. The region forms a membrane surface helix at both high and low pH, although the arrangement of the monomers within the tetramer changes with pH. Both electrophysiology and EPR data point to a critical role for residue Lys 49.
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