2KJ1
cytoplasmic domain structure of BM2 proton channel from influenza B virus
Summary for 2KJ1
| Entry DOI | 10.2210/pdb2kj1/pdb |
| Descriptor | BM2 protein (1 entity in total) |
| Functional Keywords | bm2, influenza b, cytoplasmic domain, coiled coil, transport protein |
| Biological source | Influenza B virus |
| Total number of polymer chains | 4 |
| Total formula weight | 41479.66 |
| Authors | Wang, J.,Pielak, R.,McClintock, M.,Chou, J. (deposition date: 2009-05-13, release date: 2009-11-10, Last modification date: 2024-05-22) |
| Primary citation | Wang, J.,Pielak, R.M.,McClintock, M.A.,Chou, J.J. Solution structure and functional analysis of the influenza B proton channel. Nat.Struct.Mol.Biol., 16:1267-1271, 2009 Cited by PubMed Abstract: Influenza B virus contains an integral membrane protein, BM2, that oligomerizes in the viral membrane to form a pH-activated proton channel. Here we report the solution structures of both the membrane-embedded channel domain and the cytoplasmic domain of BM2. The channel domain assumes a left-handed coiled-coil tetramer formation with a helical packing angle of -37 degrees to form a polar pore in the membrane for conducting ions. Mutagenesis and proton flux experiments identified residues involved in proton relay and suggest a mechanism of proton conductance. The cytoplasmic domain of BM2 also forms a coiled-coil tetramer. It has a bipolar charge distribution, in which a negatively charged region interacts specifically with the M1 matrix protein that is involved in packaging the genome in the virion. This interaction suggests BM2 also recruits matrix proteins to the cell surface during virus budding, making BM2 an unusual membrane protein with the dual roles of conducting ions and recruiting proteins to the membrane. PubMed: 19898475DOI: 10.1038/nsmb.1707 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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