5WUE
Structural basis for conductance through TRIC cation channels
Summary for 5WUE
| Entry DOI | 10.2210/pdb5wue/pdb |
| Related | 5WUC 5WUD 5WUF |
| Descriptor | Uncharacterized protein, SULFATE 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 | 25812.99 |
| 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: 2017-06-21, Last modification date: 2023-11-08) |
| 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 Cited by 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: 28524849DOI: 10.1038/ncomms15103 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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