A binding-block ion selective mechanism revealed by a Na/K selective channel
Yu, Jie6; Zhang, Bing1,2,4; Zhang, Yixiao6; Xu, Cong-qiao3,5; Zhuo, Wei6; Ge, Jingpeng6; Li, Jun3,5; Gao, Ning6; Li, Yang4; Yang, Maojun6
刊名PROTEIN & CELL
2018-07
卷号9期号:7页码:629-639
关键词cryo-EM MscS Na+/K+ selective channel
ISSN号1674-800X
DOI10.1007/s13238-017-0465-8
文献子类Article
英文摘要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 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(Met158)) 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(Met158) 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.
资助项目Ministry of Science and Technology[2016YFA0501100] ; Ministry of Science and Technology[2017YFA0504600] ; Ministry of Science and Technology[2016YFA0500700] ; Ministry of Science and Technology[2013CB910400] ; National Fund for Distinguished Young Scholar[31625008] ; National Natural Science Foundation of China[21532004] ; National Natural Science Foundation of China[31570733] ; National Natural Science Foundation of China[31422016] ; National Natural Science Foundation of China[31371066] ; National Natural Science Foundation of China[31671049] ; National Natural Science Foundation of China[91426302]
WOS关键词GATED SODIUM-CHANNEL ; CRYOELECTRON MICROSCOPY STRUCTURE ; CRYSTAL-STRUCTURE ; MECHANOSENSITIVE CHANNEL ; K+ CHANNEL ; CRYO-EM ; RESOLUTION ; COMPLEX ; MSCS ; ARCHITECTURE
WOS研究方向Cell Biology
语种英语
CSCD记录号CSCD:6321830
出版者HIGHER EDUCATION PRESS
WOS记录号WOS:000436455300004
内容类型期刊论文
源URL[http://119.78.100.183/handle/2S10ELR8/279687]  
专题药理学第二研究室
通讯作者Gao, Ning; Li, Yang; Yang, Maojun
作者单位1.Tongji Univ, Sch Med, Shanghai Matern & Infant Hosp 1, Anesthesiol, Shanghai 201203, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China;
3.Tsinghua Univ, Minist Educ, Key Lab Organ Optoelect & Mol Engn, Beijing 100084, Peoples R China;
4.Chinese Acad Sci, Shanghai Inst Mat Med, Key Lab Receptor Res, Shanghai 201203, Peoples R China;
5.Tsinghua Univ, Dept Chem, Beijing 100084, Peoples R China;
6.Tsinghua Univ, Beijing Adv Innovat Ctr Struct Biol, Minist Educ, Key Lab Prot Sci,Sch Life Sci,Tsinghua Peking Joi, Beijing 100084, Peoples R China;
推荐引用方式
GB/T 7714
Yu, Jie,Zhang, Bing,Zhang, Yixiao,et al. A binding-block ion selective mechanism revealed by a Na/K selective channel[J]. PROTEIN & CELL,2018,9(7):629-639.
APA Yu, Jie.,Zhang, Bing.,Zhang, Yixiao.,Xu, Cong-qiao.,Zhuo, Wei.,...&Yang, Maojun.(2018).A binding-block ion selective mechanism revealed by a Na/K selective channel.PROTEIN & CELL,9(7),629-639.
MLA Yu, Jie,et al."A binding-block ion selective mechanism revealed by a Na/K selective channel".PROTEIN & CELL 9.7(2018):629-639.
个性服务
查看访问统计
相关权益政策
暂无数据
收藏/分享
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。


©版权所有 ©2017 CSpace - Powered by CSpace