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Structural basis for conductance through TRIC cation channels
Mammalian TRICs function as K(+)-permeable cation channels that provide counter ions for Ca(2+) 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...
Autores principales: | , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5477506/ https://www.ncbi.nlm.nih.gov/pubmed/28524849 http://dx.doi.org/10.1038/ncomms15103 |
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author | Su, Min Gao, Feng Yuan, Qi Mao, Yang Li, De-lin Guo, Youzhong Yang, Cheng Wang, Xiao-hui Bruni, Renato Kloss, Brian Zhao, Hong Zeng, Yang Zhang, Fa-ben Marks, Andrew R Hendrickson, Wayne A Chen, Yu-hang |
author_facet | Su, Min Gao, Feng Yuan, Qi Mao, Yang Li, De-lin Guo, Youzhong Yang, Cheng Wang, Xiao-hui Bruni, Renato Kloss, Brian Zhao, Hong Zeng, Yang Zhang, Fa-ben Marks, Andrew R Hendrickson, Wayne A Chen, Yu-hang |
author_sort | Su, Min |
collection | PubMed |
description | Mammalian TRICs function as K(+)-permeable cation channels that provide counter ions for Ca(2+) 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. |
format | Online Article Text |
id | pubmed-5477506 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-54775062017-07-03 Structural basis for conductance through TRIC cation channels Su, Min Gao, Feng Yuan, Qi Mao, Yang Li, De-lin Guo, Youzhong Yang, Cheng Wang, Xiao-hui Bruni, Renato Kloss, Brian Zhao, Hong Zeng, Yang Zhang, Fa-ben Marks, Andrew R Hendrickson, Wayne A Chen, Yu-hang Nat Commun Article Mammalian TRICs function as K(+)-permeable cation channels that provide counter ions for Ca(2+) 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. Nature Publishing Group 2017-05-19 /pmc/articles/PMC5477506/ /pubmed/28524849 http://dx.doi.org/10.1038/ncomms15103 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Su, Min Gao, Feng Yuan, Qi Mao, Yang Li, De-lin Guo, Youzhong Yang, Cheng Wang, Xiao-hui Bruni, Renato Kloss, Brian Zhao, Hong Zeng, Yang Zhang, Fa-ben Marks, Andrew R Hendrickson, Wayne A Chen, Yu-hang Structural basis for conductance through TRIC cation channels |
title | Structural basis for conductance through TRIC cation channels |
title_full | Structural basis for conductance through TRIC cation channels |
title_fullStr | Structural basis for conductance through TRIC cation channels |
title_full_unstemmed | Structural basis for conductance through TRIC cation channels |
title_short | Structural basis for conductance through TRIC cation channels |
title_sort | structural basis for conductance through tric cation channels |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5477506/ https://www.ncbi.nlm.nih.gov/pubmed/28524849 http://dx.doi.org/10.1038/ncomms15103 |
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