2ATK

Structure of a mutant KcsA K+ channel

Summary for 2ATK

• Entry DOI: 10.2210/pdb2atk/pdb
• Related: 1ZWI
• Descriptor: ANTIBODY FAB FRAGMENT HEAVY CHAIN, ANTIBODY FAB FRAGMENT LIGHT CHAIN, Voltage-gated potassium channel, ... (6 entities in total)
• Functional Keywords: k+ channel, mutant kcsa, protein-antibody fab complex, immune system-ion transport complex, immune system/ion transport
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cell membrane; Multi-pass membrane protein: P0A334
• Total number of polymer chains: 3
• Total formula weight: 60418.47

Authors

Cordero-Morales, J.F.,Cuello, L.G.,Zhao, Y.,Jogini, V.,Chakrapani, S.,Roux, B.,Perozo, E. (deposition date: 2005-08-25, release date: 2006-03-07, Last modification date: 2024-10-23)

Primary citation

Cordero-Morales, J.F.,Cuello, L.G.,Zhao, Y.,Jogini, V.,Cortes, D.M.,Roux, B.,Perozo, E.
Molecular determinants of gating at the potassium-channel selectivity filter.
Nat.Struct.Mol.Biol., 13:311-318, 2006

PubMed Abstract: We show that in the potassium channel KcsA, proton-dependent activation is followed by an inactivation process similar to C-type inactivation, and this process is suppressed by an E71A mutation in the pore helix. EPR spectroscopy demonstrates that the inner gate opens maximally at low pH regardless of the magnitude of the single-channel-open probability, implying that stationary gating originates mostly from rearrangements at the selectivity filter. Two E71A crystal structures obtained at 2.5 A reveal large structural excursions of the selectivity filter during ion conduction and provide a glimpse of the range of conformations available to this region of the channel during gating. These data establish a mechanistic basis for the role of the selectivity filter during channel activation and inactivation.

PubMed: 16532009
DOI: 10.1038/nsmb1069

Experimental method

X-RAY DIFFRACTION (2.5 Å)