6PVT
Influenza B M2 Proton Channel in the Open State - SSNMR Structure at pH 4.5
Summary for 6PVT
| Entry DOI | 10.2210/pdb6pvt/pdb |
| NMR Information | BMRB: 30646 |
| Descriptor | BM2 protein (1 entity in total) |
| Functional Keywords | proton channel, closed state, four helix bundle, viral protein |
| Biological source | Influenza B virus (B/Maryland/1/2001) |
| Total number of polymer chains | 4 |
| Total formula weight | 23812.58 |
| Authors | Mandala, V.S.,Loftis, A.R.,Shcherbakov, A.S.,Pentelute, B.L.,Hong, M. (deposition date: 2019-07-21, release date: 2020-02-05, Last modification date: 2024-05-15) |
| Primary citation | Mandala, V.S.,Loftis, A.R.,Shcherbakov, A.A.,Pentelute, B.L.,Hong, M. Atomic structures of closed and open influenza B M2 proton channel reveal the conduction mechanism. Nat.Struct.Mol.Biol., 27:160-167, 2020 Cited by PubMed 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. PubMed: 32015551DOI: 10.1038/s41594-019-0371-2 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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