Molecular Basis of Tetramerization and pH-Gating in the KcsA Potassium Channel Cytoplasmic Domain

Guy Kamnesky; Orel Hirschhorn; Hadassa Shaked; Jingfei Chen; Lishan Yao; Jordan H. Chill

Molecular Basis of Tetramerization and pH-Gating in the KcsA Potassium Channel Cytoplasmic Domain

Guy Kamnesky, Orel Hirschhorn, Hadassa Shaked, Jingfei Chen, Lishan Yao, Jordan H. Chill

Department of Chemistry

Bar-Ilan University

Research output: Contribution to conference › Paper › peer-review

Abstract

The intracellular C-terminal domain (CTD) of KcsA, a bacterial homotetrameric potassium channel, is a 40-residue long segment which natively adopts a helical bundle conformation with four-fold symmetry. A hallmark of KcsA behavior is a pH-induced conformational change which leads to opening of the channel at acidic pH. While crystal structures of full-length KcsA failed to observe a pH-effect upon the CTD, other biophysical methods have presented evidence to the contrary. We approached the question of CTD structure and its pH-dependence by studying the behavior of soluble peptides corresponding to residues 128-160 of the CTD (CTD34).

Original language	American English
State	Published - 2015
Event	59th Biophysical Society meeting - Baltimore, United States Duration: 7 Feb 2015 → 11 Feb 2015

Conference

Conference	59th Biophysical Society meeting
Country/Territory	United States
City	Baltimore
Period	7/02/15 → 11/02/15

Cite this

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title = "Molecular Basis of Tetramerization and pH-Gating in the KcsA Potassium Channel Cytoplasmic Domain",

abstract = "The intracellular C-terminal domain (CTD) of KcsA, a bacterial homotetrameric potassium channel, is a 40-residue long segment which natively adopts a helical bundle conformation with four-fold symmetry. A hallmark of KcsA behavior is a pH-induced conformational change which leads to opening of the channel at acidic pH. While crystal structures of full-length KcsA failed to observe a pH-effect upon the CTD, other biophysical methods have presented evidence to the contrary. We approached the question of CTD structure and its pH-dependence by studying the behavior of soluble peptides corresponding to residues 128-160 of the CTD (CTD34).",

author = "Guy Kamnesky and Orel Hirschhorn and Hadassa Shaked and Jingfei Chen and Lishan Yao and Chill, {Jordan H.}",

year = "2015",

language = "American English",

note = "59th Biophysical Society meeting ; Conference date: 07-02-2015 Through 11-02-2015",

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TY - CONF

T1 - Molecular Basis of Tetramerization and pH-Gating in the KcsA Potassium Channel Cytoplasmic Domain

AU - Kamnesky, Guy

AU - Hirschhorn, Orel

AU - Shaked, Hadassa

AU - Chen, Jingfei

AU - Yao, Lishan

AU - Chill, Jordan H.

PY - 2015

Y1 - 2015

N2 - The intracellular C-terminal domain (CTD) of KcsA, a bacterial homotetrameric potassium channel, is a 40-residue long segment which natively adopts a helical bundle conformation with four-fold symmetry. A hallmark of KcsA behavior is a pH-induced conformational change which leads to opening of the channel at acidic pH. While crystal structures of full-length KcsA failed to observe a pH-effect upon the CTD, other biophysical methods have presented evidence to the contrary. We approached the question of CTD structure and its pH-dependence by studying the behavior of soluble peptides corresponding to residues 128-160 of the CTD (CTD34).

AB - The intracellular C-terminal domain (CTD) of KcsA, a bacterial homotetrameric potassium channel, is a 40-residue long segment which natively adopts a helical bundle conformation with four-fold symmetry. A hallmark of KcsA behavior is a pH-induced conformational change which leads to opening of the channel at acidic pH. While crystal structures of full-length KcsA failed to observe a pH-effect upon the CTD, other biophysical methods have presented evidence to the contrary. We approached the question of CTD structure and its pH-dependence by studying the behavior of soluble peptides corresponding to residues 128-160 of the CTD (CTD34).

UR - https://www.biophysics.org/past-annual-meetings/59th-annual-meeting

M3 - Paper

T2 - 59th Biophysical Society meeting

Y2 - 7 February 2015 through 11 February 2015

ER -

Molecular Basis of Tetramerization and pH-Gating in the KcsA Potassium Channel Cytoplasmic Domain

Abstract

Conference

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