5HVX
Full length Wild-Type Open-form Sodium Channel NavMs
Summary for 5HVX
| Entry DOI | 10.2210/pdb5hvx/pdb |
| Descriptor | Ion transport protein, SODIUM ION, HEGA-10, ... (7 entities in total) |
| Functional Keywords | integral membrane full length voltage gated sodium channel transport, transport protein |
| Biological source | Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1) |
| Total number of polymer chains | 1 |
| Total formula weight | 32667.39 |
| Authors | Sula, A.,Booker, J.E.,Naylor, C.E.,Wallace, B.A. (deposition date: 2016-01-28, release date: 2017-03-01, Last modification date: 2024-01-10) |
| Primary citation | Sula, A.,Booker, J.,Ng, L.C.,Naylor, C.E.,DeCaen, P.G.,Wallace, B.A. The complete structure of an activated open sodium channel. Nat Commun, 8:14205-14205, 2017 Cited by PubMed Abstract: Voltage-gated sodium channels (Navs) play essential roles in excitable tissues, with their activation and opening resulting in the initial phase of the action potential. The cycling of Navs through open, closed and inactivated states, and their closely choreographed relationships with the activities of other ion channels lead to exquisite control of intracellular ion concentrations in both prokaryotes and eukaryotes. Here we present the 2.45 Å resolution crystal structure of the complete NavMs prokaryotic sodium channel in a fully open conformation. A canonical activated conformation of the voltage sensor S4 helix, an open selectivity filter leading to an open activation gate at the intracellular membrane surface and the intracellular C-terminal domain are visible in the structure. It includes a heretofore unseen interaction motif between W77 of S3, the S4-S5 interdomain linker, and the C-terminus, which is associated with regulation of opening and closing of the intracellular gate. PubMed: 28205548DOI: 10.1038/ncomms14205 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.45 Å) |
Structure validation
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