Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel
Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel
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DOI：
10.1016/s0896-6273(01)00236-7
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发表时间：
2001-03-01
期刊：
影响因子：
16.2
通讯作者：
MacKinnon, R
中科院分区：
文献类型：
--
作者：
Jiang, YX;Pico, A;MacKinnon, R
用2.4埃分辨率的X射线结晶学研究了大肠杆菌六跨膜钾通道的胞内C-末端结构域结构。这种结构代表了原核生物K+转运体和K+通道中调节K+电导的一大类结构域/蛋白质(称为RCK结构域)。RCK结构域具有独特的位置的Rossmann折叠拓扑结构，在Rossmann折叠蛋白中并不常见，由一个保守的盐桥和一个疏水的二聚体界面组成。基于结构的氨基酸序列比对和突变分析表明，RCK结构域也存在，是真核细胞大电导钙激活K+通道门控机制的重要组成部分。
The intracellular C-terminal domain structure of a six-transmembrane K+ channel from Escherichia coli has been solved by X-ray crystallography at 2.4 Angstrom resolution. The structure is representative of a broad class of domains/proteins that regulate the conductance of K+ there referred to as RCK domains) in prokaryotic K+ transporters and K+ channels. The RCK domain has a Rossmann-fold topology with unique positions, not commonly conserved among Rossmann-fold proteins, composing a well-conserved salt bridge and a hydrophobic dimer interface. Structure-based amino acid sequence alignments and mutational analysis are used to demonstrate that an RCK domain is also present and is an important component of the gating machinery in eukaryotic large-conductance Ca2+-activated K+ channels.