PDBsum entry 5k7l

Metal transport/calcium binding protein

PDB id: 5k7l

Contents

Protein chains

701 a.a.

142 a.a.

Ligands

NAG

Y01

PDB id:

5k7l

Name:

Metal transport/calcium binding protein

Title:

Single particle cryo-em structure of the voltage-gated k+ channel eag1 bound to the channel inhibitor calmodulin

Structure:

Potassium voltage-gated channel subfamily h member 1. Chain: a. Fragment: unp residues 1-773, 888-962. Synonym: voltage-gated potassium channel eag1, ether-a-go-go potassium channel 1, r-eag, voltage-gated potassium channel subunit kv10.1. Engineered: yes. Calmodulin. Chain: b.

Source:

Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: kcnh1, eag. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293 gnti-. Homo sapiens. Human.

Authors:

J.R.Whicher,R.Mackinnon

Key ref:

J.R.Whicher and R.MacKinnon (2016). Structure of the voltage-gated K⁺ channel Eag1 reveals an alternative voltage sensing mechanism. Science, 353, 664-669. PubMed id: 27516594 DOI: 10.1126/science.aaf8070

Date:

26-May-16 Release date: 17-Aug-16

Protein chain

Q63472  (KCNH1_RAT) -  Voltage-gated delayed rectifier potassium channel KCNH1 from Rattus norvegicus

Seq: 962 a.a.

Struc: 701 a.a.

Protein chain

P0DP23  (CALM1_HUMAN) -  Calmodulin-1 from Homo sapiens

Seq: 149 a.a.

Struc: 142 a.a.

DOI no: 10.1126/science.aaf8070

Science 353:664-669 (2016)

PubMed id: 27516594

Structure of the voltage-gated K⁺ channel Eag1 reveals an alternative voltage sensing mechanism.

J.R.Whicher, R.MacKinnon.

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.