scholarly journals Discovery and characterisation of a novel toxin from Dendroaspis angusticeps, named Tx7335, that activates the potassium channel KcsA

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Iván O. Rivera-Torres ◽  
Tony B. Jin ◽  
Martine Cadene ◽  
Brian T. Chait ◽  
Sébastien F. Poget
Keyword(s):  
Potassium Channel ◽  
Dendroaspis Angusticeps ◽  
Potassium Channel Kcsa

scholarly journals Characterizing the Fatty Acid Binding Site in the Cavity of Potassium Channel KcsA

Biochemistry ◽  
2012 ◽  
Vol 51 (40) ◽  
pp. 7996-8002 ◽  
Author(s):  
Natalie Smithers ◽  
Juan H. Bolivar ◽  
Anthony G. Lee ◽  
J. Malcolm East
Keyword(s):  
Fatty Acid ◽  
Potassium Channel ◽  
Binding Site ◽  
Fatty Acid Binding ◽  
Potassium Channel Kcsa ◽  
Fatty Acid Binding Site

scholarly journals Local and global structure of the monomeric subunit of the potassium channel KcsA probed by NMR

2007 ◽  
Vol 1768 (12) ◽  
pp. 3260-3270 ◽  
Author(s):  
Jordan H. Chill ◽  
John M. Louis ◽  
Frank Delaglio ◽  
Ad Bax
Keyword(s):  
Potassium Channel ◽  
Global Structure ◽  
Potassium Channel Kcsa

scholarly journals Inactivation in the potassium channel KcsA

2019 ◽  
Vol 3 ◽  
pp. 100009 ◽  
Author(s):  
Yunyao Xu ◽  
Ann E. McDermott
Keyword(s):  
Potassium Channel ◽  
Potassium Channel Kcsa

Effects of Lipid Structure on the State of Aggregation of Potassium Channel KcsA

Biochemistry ◽  
2012 ◽  
Vol 51 (30) ◽  
pp. 6010-6016 ◽  
Author(s):  
Juan H. Bolivar ◽  
J. Malcolm East ◽  
Derek Marsh ◽  
Anthony G. Lee
Keyword(s):  
Potassium Channel ◽  
The State ◽  
Lipid Structure ◽  
Potassium Channel Kcsa

Unfolding and Refolding in Vitro of a Tetrameric, α-Helical Membrane Protein:  The Prokaryotic Potassium Channel KcsA†

Biochemistry ◽  
2005 ◽  
Vol 44 (43) ◽  
pp. 14344-14352 ◽  
Author(s):  
Francisco N. Barrera ◽  
M. Lourdes Renart ◽  
M. Luisa Molina ◽  
José A. Poveda ◽  
José A. Encinar ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Potassium Channel ◽  
Potassium Channel Kcsa

scholarly journals Phosphatidic acid plays a special role in stabilizing and folding of the tetrameric potassium channel KcsA

FEBS Letters ◽  
2007 ◽  
Vol 581 (29) ◽  
pp. 5715-5722 ◽  
Author(s):  
Mobeen Raja ◽  
Robin E.J. Spelbrink ◽  
Ben de Kruijff ◽  
J. Antoinette Killian
Keyword(s):  
Phosphatidic Acid ◽  
Potassium Channel ◽  
Special Role ◽  
Potassium Channel Kcsa

scholarly journals Normal-Mode Refinement of Anisotropic Thermal Parameters for Potassium Channel KcsA at 3.2 Å Crystallographic Resolution

Structure ◽  
2007 ◽  
Vol 15 (8) ◽  
pp. 955-962 ◽  
Author(s):  
Xiaorui Chen ◽  
Billy K. Poon ◽  
Athanasios Dousis ◽  
Qinghua Wang ◽  
Jianpeng Ma
Keyword(s):  
Potassium Channel ◽  
Normal Mode ◽  
Thermal Parameters ◽  
Potassium Channel Kcsa

scholarly journals Conformational heterogeneity in closed and open states of the KcsA potassium channel in lipid bicelles

2016 ◽  
Vol 148 (2) ◽  
pp. 119-132 ◽  
Author(s):  
Dorothy M. Kim ◽  
Igor Dikiy ◽  
Vikrant Upadhyay ◽  
David J. Posson ◽  
David Eliezer ◽  
...  
Keyword(s):  
Ion Channel ◽  
Potassium Channel ◽  
Conformational Changes ◽  
Ph Dependence ◽  
Channel Gating ◽  
Conformational Heterogeneity ◽  
Ion Channel Gating ◽  
Potassium Channel Kcsa ◽  
Functional States ◽  
Open States

The process of ion channel gating—opening and closing—involves local and global structural changes in the channel in response to external stimuli. Conformational changes depend on the energetic landscape that underlies the transition between closed and open states, which plays a key role in ion channel gating. For the prokaryotic, pH-gated potassium channel KcsA, closed and open states have been extensively studied using structural and functional methods, but the dynamics within each of these functional states as well as the transition between them is not as well understood. In this study, we used solution nuclear magnetic resonance (NMR) spectroscopy to investigate the conformational transitions within specific functional states of KcsA. We incorporated KcsA channels into lipid bicelles and stabilized them into a closed state by using either phosphatidylcholine lipids, known to favor the closed channel, or mutations designed to trap the channel shut by disulfide cross-linking. A distinct state, consistent with an open channel, was uncovered by the addition of cardiolipin lipids. Using selective amino acid labeling at locations within the channel that are known to move during gating, we observed at least two different slowly interconverting conformational states for both closed and open channels. The pH dependence of these conformations and the predictable disruptions to this dependence observed in mutant channels with altered pH sensing highlight the importance of conformational heterogeneity for KcsA gating.

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