7UX1

EcMscK in an Open Conformation

Summary for 7UX1

• Entry DOI: 10.2210/pdb7ux1/pdb
• EMDB information: 26823 26845 26851 26854
• Descriptor: Mechanosensitive channel MscK (1 entity in total)
• Functional Keywords: membrane protein, mechanosensation, ion channel, transport protein
• 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: 2022-05-04, 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

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: 36371466
DOI: 10.1038/s41467-022-34737-0

Experimental method

ELECTRON MICROSCOPY (3.48 Å)