Structural basis for conductance through TRIC cation channels

Min Su (), Feng Gao (), Qi Yuan (), Yang Mao (), Li De-lin (), Youzhong Guo, Cheng Yang, Xiao-hui Wang, Renato Bruni, Brian Kloss, Hong Zhao, Yang Zeng, Fa-ben Zhang, Andrew R Marks, Wayne A Hendrickson () and Yu-hang Chen ()
Additional contact information
Min Su: State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences
Feng Gao: State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences
Qi Yuan: Columbia University
Yang Mao: State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences
Li De-lin: University of Chinese Academy of Sciences
Youzhong Guo: Columbia University
Cheng Yang: State Key Laboratory of Medicinal Chemical Biology, College of Pharmacy and Tianjin Key Laboratory of Molecular Drug Research, Nankai University
Xiao-hui Wang: University of Chinese Academy of Sciences
Renato Bruni: Center on Membrane Protein Production and Analysis, New York Structural Biology Center
Brian Kloss: Center on Membrane Protein Production and Analysis, New York Structural Biology Center
Hong Zhao: State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences
Yang Zeng: University of Chinese Academy of Sciences
Fa-ben Zhang: University of Chinese Academy of Sciences
Andrew R Marks: Columbia University
Wayne A Hendrickson: Columbia University
Yu-hang Chen: State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences

Nature Communications, 2017, vol. 8, issue 1, 1-13

Abstract: Abstract Mammalian TRICs function as K+-permeable cation channels that provide counter ions for Ca2+ handling in intracellular stores. Here we describe the structures of two prokaryotic homologues, archaeal SaTRIC and bacterial CpTRIC, showing that TRIC channels are symmetrical trimers with transmembrane pores through each protomer. Each pore holds a string of water molecules centred at kinked helices in two inverted-repeat triple-helix bundles (THBs). The pores are locked in a closed state by a hydrogen bond network at the C terminus of the THBs, which is lost when the pores assume an open conformation. The transition between the open and close states seems to be mediated by cation binding to conserved residues along the three-fold axis. Electrophysiology and mutagenesis studies show that prokaryotic TRICs have similar functional properties to those of mammalian TRICs and implicate the three-fold axis in the allosteric regulation of the channel.

Date: 2017
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DOI: 10.1038/ncomms15103

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