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Atomic structures of closed and open influenza B M2 proton channel reveal the conduction mechanism.

ABSTRACT: The influenza B M2 (BM2) proton channel is activated by acidic pH to mediate virus uncoating. Unlike influenza A M2 (AM2), which conducts protons with strong inward rectification, BM2 conducts protons both inward and outward. Here we report 1.4- and 1.5-Å solid-state NMR structures of the transmembrane domain of the closed and open BM2 channels in a phospholipid environment. Upon activation, the transmembrane helices increase the tilt angle by 6° and the average pore diameter enlarges by 2.1?Å. BM2 thus undergoes a scissor motion for activation, which differs from the alternating-access motion of AM2. These results indicate that asymmetric proton conduction requires a backbone hinge motion, whereas bidirectional conduction is achieved by a symmetric scissor motion. The proton-selective histidine and gating tryptophan in the open BM2 reorient on the microsecond timescale, similar to AM2, indicating that side chain dynamics are the essential driver of proton shuttling.

SUBMITTER: Mandala VS 

PROVIDER: S-EPMC7641042 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature

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Atomic structures of closed and open influenza B M2 proton channel reveal the conduction mechanism.

Mandala Venkata S VS   Loftis Alexander R AR   Shcherbakov Alexander A AA   Pentelute Bradley L BL   Hong Mei M  

Nature structural & molecular biology 20200203 2

The influenza B M2 (BM2) proton channel is activated by acidic pH to mediate virus uncoating. Unlike influenza A M2 (AM2), which conducts protons with strong inward rectification, BM2 conducts protons both inward and outward. Here we report 1.4- and 1.5-Å solid-state NMR structures of the transmembrane domain of the closed and open BM2 channels in a phospholipid environment. Upon activation, the transmembrane helices increase the tilt angle by 6° and the average pore diameter enlarges by 2.1 Å.  ...[more]

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