» Articles » PMID: 19346472

Crystal Structure of Full-length KcsA in Its Closed Conformation

Overview
Specialty Science
Date 2009 Apr 7
PMID 19346472
Citations 138
Authors
Affiliations
Soon will be listed here.
Abstract

KcsA is a proton-activated, voltage-modulated K(+) channel that has served as the archetype pore domain in the Kv channel superfamily. Here, we have used synthetic antigen-binding fragments (Fabs) as crystallographic chaperones to determine the structure of full-length KcsA at 3.8 A, as well as that of its isolated C-terminal domain at 2.6 A. The structure of the full-length KcsA-Fab complex reveals a well-defined, 4-helix bundle that projects approximately 70 A toward the cytoplasm. This bundle promotes a approximately 15 degree bending in the inner bundle gate, tightening its diameter and shifting the narrowest point 2 turns of helix below. Functional analysis of the full-length KcsA-Fab complex suggests that the C-terminal bundle remains whole during gating. We suggest that this structure likely represents the physiologically relevant closed conformation of KcsA.

Citing Articles

Mediation of mammalian olfactory response by presence of odor-evoked potassium current.

Hagerty S, Pustovyy O, Globa L, Vodyanoy V, Singletary M Front Allergy. 2024; 5:1478529.

PMID: 39479387 PMC: 11521970. DOI: 10.3389/falgy.2024.1478529.


Conformational Dynamic Studies of Prokaryotic Potassium Channels Explored by Homo-FRET Methodologies.

Coutinho A, Poveda J, Renart M Methods Mol Biol. 2024; 2796:35-72.

PMID: 38856894 DOI: 10.1007/978-1-0716-3818-7_3.


Cardiolipin binding enhances KcsA channel gating via both its specific and dianion-monoanion interchangeable sites.

Iwamoto M, Morito M, Oiki S, Nishitani Y, Yamamoto D, Matsumori N iScience. 2023; 26(12):108471.

PMID: 38077151 PMC: 10709135. DOI: 10.1016/j.isci.2023.108471.


Anionic Phospholipids Shift the Conformational Equilibrium of the Selectivity Filter in the KcsA Channel to the Conductive Conformation: Predicted Consequences on Inactivation.

Renart M, Giudici A, Coll-Diez C, Gonzalez-Ros J, Poveda J Biomedicines. 2023; 11(5).

PMID: 37239046 PMC: 10216125. DOI: 10.3390/biomedicines11051376.


Bacterial spore germination receptors are nutrient-gated ion channels.

Gao Y, Amon J, Artzi L, Ramirez-Guadiana F, Brock K, Cofsky J Science. 2023; 380(6643):387-391.

PMID: 37104613 PMC: 11154005. DOI: 10.1126/science.adg9829.


References
1.
Jiang Y, Lee A, Chen J, Cadene M, Chait B, MacKinnon R . Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 2002; 417(6888):515-22. DOI: 10.1038/417515a. View

2.
Ye J, Tereshko V, Frederiksen J, Koide A, Fellouse F, Sidhu S . Synthetic antibodies for specific recognition and crystallization of structured RNA. Proc Natl Acad Sci U S A. 2007; 105(1):82-7. PMC: 2224236. DOI: 10.1073/pnas.0709082105. View

3.
Rapp C, Pollack R . Crystal packing effects on protein loops. Proteins. 2005; 60(1):103-9. DOI: 10.1002/prot.20492. View

4.
Unwin N . Refined structure of the nicotinic acetylcholine receptor at 4A resolution. J Mol Biol. 2005; 346(4):967-89. DOI: 10.1016/j.jmb.2004.12.031. View

5.
Cordero-Morales J, Cuello L, Perozo E . Voltage-dependent gating at the KcsA selectivity filter. Nat Struct Mol Biol. 2006; 13(4):319-22. DOI: 10.1038/nsmb1070. View