2L0J
Solid State NMR structure of the M2 proton channel from Influenza A Virus in hydrated lipid bilayer
Summary for 2L0J
| Entry DOI | 10.2210/pdb2l0j/pdb |
| Descriptor | Matrix protein 2 (1 entity in total) |
| Functional Keywords | m2 proton channel, lipid bilayer, solid state nmr, influenza, conductance domain, membrane domain, viral protein, transport protein |
| Biological source | Influenza A virus |
| Cellular location | Virion membrane (By similarity): P63231 |
| Total number of polymer chains | 4 |
| Total formula weight | 20087.70 |
| Authors | Sharma, M.,Yi, M.,Dong, H.,Qin, H.,Peterson, E.,Busath, D.D.,Zhou, H.X.,Cross, T.A. (deposition date: 2010-07-08, release date: 2010-11-03, Last modification date: 2024-05-01) |
| Primary citation | Sharma, M.,Yi, M.,Dong, H.,Qin, H.,Peterson, E.,Busath, D.D.,Zhou, H.X.,Cross, T.A. Insight into the mechanism of the influenza a proton channel from a structure in a lipid bilayer. Science, 330:509-512, 2010 Cited by PubMed Abstract: The M2 protein from the influenza A virus, an acid-activated proton-selective channel, has been the subject of numerous conductance, structural, and computational studies. However, little is known at the atomic level about the heart of the functional mechanism for this tetrameric protein, a His(37)-Trp(41) cluster. We report the structure of the M2 conductance domain (residues 22 to 62) in a lipid bilayer, which displays the defining features of the native protein that have not been attainable from structures solubilized by detergents. We propose that the tetrameric His(37)-Trp(41) cluster guides protons through the channel by forming and breaking hydrogen bonds between adjacent pairs of histidines and through specific interactions of the histidines with the tryptophan gate. This mechanism explains the main observations on M2 proton conductance. PubMed: 20966252DOI: 10.1126/science.1191750 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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