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5Y4O

Cryo-EM structure of MscS channel, YnaI

Summary for 5Y4O
Entry DOI10.2210/pdb5y4o/pdb
EMDB information6805
DescriptorLow conductance mechanosensitive channel YnaI (1 entity in total)
Functional Keywordscryo-em, mscs, na/k selective channel, membrane protein
Biological sourceEscherichia coli O157:H7
Total number of polymer chains7
Total formula weight277348.51
Authors
Zhang, Y.,Yu, J. (deposition date: 2017-08-04, release date: 2019-03-20, Last modification date: 2024-10-16)
Primary citationYu, 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: 28921397
DOI: 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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数据于2025-07-23公开中

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