7UW5
EcMscK G924S mutant in a closed conformation
Summary for 7UW5
| Entry DOI | 10.2210/pdb7uw5/pdb |
| EMDB information | 26823 |
| Descriptor | Mechanosensitive channel MscK (1 entity in total) |
| Functional Keywords | transport protein, membrane protein, mechanosensation, ion channel |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 7 |
| Total formula weight | 891651.52 |
| Authors | Mount, J.W.,Yuan, P. (deposition date: 2022-05-02, release date: 2022-11-23, Last modification date: 2024-06-12) |
| Primary citation | Mount, J.,Maksaev, G.,Summers, B.T.,Fitzpatrick, J.A.J.,Yuan, P. Structural basis for mechanotransduction in a potassium-dependent mechanosensitive ion channel. Nat Commun, 13:6904-6904, 2022 Cited by PubMed Abstract: Mechanosensitive channels of small conductance, found in many living organisms, open under elevated membrane tension and thus play crucial roles in biological response to mechanical stress. Amongst these channels, MscK is unique in that its activation also requires external potassium ions. To better understand this dual gating mechanism by force and ligand, we elucidate distinct structures of MscK along the gating cycle using cryo-electron microscopy. The heptameric channel comprises three layers: a cytoplasmic domain, a periplasmic gating ring, and a markedly curved transmembrane domain that flattens and expands upon channel opening, which is accompanied by dilation of the periplasmic ring. Furthermore, our results support a potentially unifying mechanotransduction mechanism in ion channels depicted as flattening and expansion of the transmembrane domain. PubMed: 36371466DOI: 10.1038/s41467-022-34737-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.84 Å) |
Structure validation
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