5WUD

Structural basis for conductance through TRIC cation channels

5WUD の概要

• エントリーDOI: 10.2210/pdb5wud/pdb
• 関連するPDBエントリー: 5WUC 5WUE 5WUF
• 分子名称: Uncharacterized protein, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: tric, cation channel, membrane protein, structural genomics, psi-biology, new york consortium on membrane protein structure, nycomps
• 由来する生物種: Sulfolobus acidocaldarius
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25741.23

構造登録者

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) (登録日: 2016-12-17, 公開日: 2017-06-21, 最終更新日: 2023-11-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)