2BOB

Potassium channel KcsA-Fab complex in thallium with tetrabutylammonium (TBA)

Summary for 2BOB

• Entry DOI: 10.2210/pdb2bob/pdb
• Related: 1BL8 1F6G 1J95 1JQ1 1JQ2 1JVM 1K4C 1K4D 1R3I 1R3J 1R3K 1R3L 1S5H
• Descriptor: ANTIBODY FAB FRAGMENT HEAVY CHAIN, ANTIBODY FAB FRAGMENT LIGHT CHAIN, POTASSIUM CHANNEL KCSA, ... (7 entities in total)
• Functional Keywords: immune system/transport protein, complex (antibody-ion channel), potassium channel, ion transport, ionic channel, protein- antibody fab complex, immune system-transport protein complex
• Biological source: STREPTOMYCES LIVIDANS; More
• Cellular location: Cell membrane; Multi-pass membrane protein: P0A334
• Total number of polymer chains: 3
• Total formula weight: 60564.34

Authors

Lenaeus, M.J.,Vamvouka, M.,Focia, P.J.,Gross, A. (deposition date: 2005-04-09, release date: 2005-04-27, Last modification date: 2024-11-20)

Primary citation

Lenaeus, M.J.,Vamvouka, M.,Focia, P.J.,Gross, A.
Structural Basis of Tea Blockade in a Model Potassium Channel
Nat.Struct.Mol.Biol., 12:454-, 2005

PubMed Abstract: Potassium channels catalyze the selective transfer of potassium across the cell membrane and are essential for setting the resting potential in cells, controlling heart rate and modulating the firing pattern in neurons. Tetraethylammonium (TEA) blocks ion conduction through potassium channels in a voltage-dependent manner from both sides of the membrane. Here we show the structural basis of TEA blockade by cocrystallizing the prokaryotic potassium channel KcsA with two selective TEA analogs. TEA binding at both sites alters ion occupancy in the selectivity filter; these findings underlie the mutual destabilization and voltage-dependence of TEA blockade. We propose that TEA blocks potassium channels by acting as a potassium analog at the dehydration transition step during permeation.

PubMed: 15852022
DOI: 10.1038/NSMB929

Experimental method

X-RAY DIFFRACTION (2.76 Å)