5Y4O
Cryo-EM structure of MscS channel, YnaI
Summary for 5Y4O
Entry DOI | 10.2210/pdb5y4o/pdb |
EMDB information | 6805 |
Descriptor | Low conductance mechanosensitive channel YnaI (1 entity in total) |
Functional Keywords | cryo-em, mscs, na/k selective channel, membrane protein |
Biological source | Escherichia coli O157:H7 |
Total number of polymer chains | 7 |
Total formula weight | 277348.51 |
Authors | |
Primary citation | Yu, J.,Zhang, B.,Zhang, Y.,Xu, C.Q.,Zhuo, W.,Ge, J.,Li, J.,Gao, N.,Li, Y.,Yang, M. A binding-block ion selective mechanism revealed by a Na/K selective channel. Protein Cell, 9:629-639, 2018 Cited by PubMed Abstract: Mechanosensitive (MS) channels are extensively studied membrane protein for maintaining intracellular homeostasis through translocating solutes and ions across the membrane, but its mechanisms of channel gating and ion selectivity are largely unknown. Here, we identified the YnaI channel as the Na/K cation-selective MS channel and solved its structure at 3.8 Å by cryo-EM single-particle method. YnaI exhibits low conductance among the family of MS channels in E. coli, and shares a similar overall heptamer structure fold with previously studied MscS channels. By combining structural based mutagenesis, quantum mechanical and electrophysiological characterizations, we revealed that ion selective filter formed by seven hydrophobic methionine (YnaI) in the transmembrane pore determined ion selectivity, and both ion selectivity and gating of YnaI channel were affected by accompanying anions in solution. Further quantum simulation and functional validation support that the distinct binding energies with various anions to YnaI facilitate Na/K pass through, which was defined as binding-block mechanism. Our structural and functional studies provided a new perspective for understanding the mechanism of how MS channels select ions driven by mechanical force. PubMed: 28921397DOI: 10.1007/s13238-017-0465-8 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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