Cargando…

Cooperative Transition between Open and Closed Conformations in Potassium Channels

Potassium (K(+)) ion channels switch between open and closed conformations. The nature of this important transition was revealed by comparing the X-ray crystal structures of the MthK channel from Methanobacterium thermoautotrophicum, obtained in its open conformation, and the KcsA channel from Strep...

Descripción completa

Detalles Bibliográficos
Autores principales: Haliloglu, Turkan, Ben-Tal, Nir
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2528004/
https://www.ncbi.nlm.nih.gov/pubmed/18769593
http://dx.doi.org/10.1371/journal.pcbi.1000164
_version_ 1782158849827930112
author Haliloglu, Turkan
Ben-Tal, Nir
author_facet Haliloglu, Turkan
Ben-Tal, Nir
author_sort Haliloglu, Turkan
collection PubMed
description Potassium (K(+)) ion channels switch between open and closed conformations. The nature of this important transition was revealed by comparing the X-ray crystal structures of the MthK channel from Methanobacterium thermoautotrophicum, obtained in its open conformation, and the KcsA channel from Streptomyces lividans, obtained in its closed conformation. We analyzed the dynamic characteristics and energetics of these homotetrameric structures in order to study the role of the intersubunit cooperativity in this transition. For this, elastic models and in silico alanine-scanning mutagenesis were used, respectively. Reassuringly, the calculations manifested motion from the open (closed) towards the closed (open) conformation. The calculations also revealed a network of dynamically and energetically coupled residues. Interestingly, the network suggests coupling between the selectivity filter and the gate, which are located at the two ends of the channel pore. Coupling between these two regions was not observed in calculations that were conducted with the monomer, which emphasizes the importance of the intersubunit interactions within the tetrameric structure for the cooperative gating behavior of the channel.
format Text
id pubmed-2528004
institution National Center for Biotechnology Information
language English
publishDate 2008
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-25280042008-09-03 Cooperative Transition between Open and Closed Conformations in Potassium Channels Haliloglu, Turkan Ben-Tal, Nir PLoS Comput Biol Research Article Potassium (K(+)) ion channels switch between open and closed conformations. The nature of this important transition was revealed by comparing the X-ray crystal structures of the MthK channel from Methanobacterium thermoautotrophicum, obtained in its open conformation, and the KcsA channel from Streptomyces lividans, obtained in its closed conformation. We analyzed the dynamic characteristics and energetics of these homotetrameric structures in order to study the role of the intersubunit cooperativity in this transition. For this, elastic models and in silico alanine-scanning mutagenesis were used, respectively. Reassuringly, the calculations manifested motion from the open (closed) towards the closed (open) conformation. The calculations also revealed a network of dynamically and energetically coupled residues. Interestingly, the network suggests coupling between the selectivity filter and the gate, which are located at the two ends of the channel pore. Coupling between these two regions was not observed in calculations that were conducted with the monomer, which emphasizes the importance of the intersubunit interactions within the tetrameric structure for the cooperative gating behavior of the channel. Public Library of Science 2008-08-29 /pmc/articles/PMC2528004/ /pubmed/18769593 http://dx.doi.org/10.1371/journal.pcbi.1000164 Text en Haliloglu, Ben-Tal. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Haliloglu, Turkan
Ben-Tal, Nir
Cooperative Transition between Open and Closed Conformations in Potassium Channels
title Cooperative Transition between Open and Closed Conformations in Potassium Channels
title_full Cooperative Transition between Open and Closed Conformations in Potassium Channels
title_fullStr Cooperative Transition between Open and Closed Conformations in Potassium Channels
title_full_unstemmed Cooperative Transition between Open and Closed Conformations in Potassium Channels
title_short Cooperative Transition between Open and Closed Conformations in Potassium Channels
title_sort cooperative transition between open and closed conformations in potassium channels
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2528004/
https://www.ncbi.nlm.nih.gov/pubmed/18769593
http://dx.doi.org/10.1371/journal.pcbi.1000164
work_keys_str_mv AT halilogluturkan cooperativetransitionbetweenopenandclosedconformationsinpotassiumchannels
AT bentalnir cooperativetransitionbetweenopenandclosedconformationsinpotassiumchannels