5WUC

Structural basis for conductance through TRIC cation channels

Summary for 5WUC

• Entry DOI: 10.2210/pdb5wuc/pdb
• Related: 5WUD 5WUE 5WUF
• Descriptor: Uncharacterized protein, SODIUM ION (3 entities in total)
• Functional Keywords: tric, cation channel, membrane protein, structural genomics, psi-biology, new york consortium on membrane protein structure, nycomps
• Biological source: Sulfolobus acidocaldarius
• Total number of polymer chains: 1
• Total formula weight: 25762.90

Authors

Su, M.,Gao, F.,Mao, Y.,Li, D.L.,Guo, Y.Z.,Wang, X.H.,Bruni, R.,Kloss, B.,Hendrickson, W.A.,Chen, Y.H.,New York Consortium on Membrane Protein Structure (NYCOMPS) (deposition date: 2016-12-17, release date: 2017-07-12, Last modification date: 2024-03-20)

Primary citation

Su, M.,Gao, F.,Yuan, Q.,Mao, Y.,Li, D.L.,Guo, Y.,Yang, C.,Wang, X.H.,Bruni, R.,Kloss, B.,Zhao, H.,Zeng, Y.,Zhang, F.B.,Marks, A.R.,Hendrickson, W.A.,Chen, Y.H.
Structural basis for conductance through TRIC cation channels.
Nat Commun, 8:15103-15103, 2017

PubMed Abstract: Mammalian TRICs function as K-permeable cation channels that provide counter ions for Ca 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.

PubMed: 28524849
DOI: 10.1038/ncomms15103

Experimental method

X-RAY DIFFRACTION (1.6 Å)