5K7L

Single particle cryo-EM structure of the voltage-gated K+ channel Eag1 bound to the channel inhibitor calmodulin

Summary for 5K7L

• Entry DOI: 10.2210/pdb5k7l/pdb
• EMDB information: 8215
• Descriptor: Potassium voltage-gated channel subfamily H member 1, Calmodulin, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: voltage-gated potassium channel, calmodulin, cryoelectron microscopy, eag1, metal transport-calcium binding protein complex, metal transport/calcium binding protein
• Biological source: Rattus norvegicus (Rat); More
• Total number of polymer chains: 2
• Total formula weight: 114920.24

Authors

Whicher, J.R.,MacKinnon, R. (deposition date: 2016-05-26, release date: 2016-08-17, Last modification date: 2024-10-23)

Primary citation

Whicher, J.R.,MacKinnon, R.
Structure of the voltage-gated K+ channel Eag1 reveals an alternative voltage sensing mechanism.
Science, 353:664-669, 2016

PubMed Abstract: Voltage-gated potassium (K(v)) channels are gated by the movement of the transmembrane voltage sensor, which is coupled, through the helical S4-S5 linker, to the potassium pore. We determined the single-particle cryo-electron microscopy structure of mammalian K(v)10.1, or Eag1, bound to the channel inhibitor calmodulin, at 3.78 angstrom resolution. Unlike previous K(v) structures, the S4-S5 linker of Eag1 is a five-residue loop and the transmembrane segments are not domain swapped, which suggest an alternative mechanism of voltage-dependent gating. Additionally, the structure and position of the S4-S5 linker allow calmodulin to bind to the intracellular domains and to close the potassium pore, independent of voltage-sensor position. The structure reveals an alternative gating mechanism for K(v) channels and provides a template to further understand the gating properties of Eag1 and related channels.

PubMed: 27516594
DOI: 10.1126/science.aaf8070

Experimental method

ELECTRON MICROSCOPY (3.78 Å)