Ontology highlight
ABSTRACT:
SUBMITTER: Su M
PROVIDER: S-EPMC5477506 | biostudies-literature | 2017 May
REPOSITORIES: biostudies-literature
Su Min M Gao Feng F Yuan Qi Q Mao Yang Y Li De-Lin DL Guo Youzhong Y Yang Cheng C Wang Xiao-Hui XH Bruni Renato R Kloss Brian B Zhao Hong H Zeng Yang Y Zhang Fa-Ben FB Marks Andrew R AR Hendrickson Wayne A WA Chen Yu-Hang YH
Nature communications 20170519
Mammalian TRICs function as K<sup>+</sup>-permeable cation channels that provide counter ions for Ca<sup>2+</sup> 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 clos ...[more]