X-ray structure of a voltage-dependent K+ channel

@article{Jiang2003XraySO,
  title={X-ray structure of a voltage-dependent K+ channel},
  author={Youxing Jiang and Alice Lee and Jiayun Chen and Vanessa Ruta and Martine Cadene and Brian T. Chait and Roderick MacKinnon},
  journal={Nature},
  year={2003},
  volume={423},
  pages={33-41}
}
Voltage-dependent K+ channels are members of the family of voltage-dependent cation (K+, Na+ and Ca2+) channels that open and allow ion conduction in response to changes in cell membrane voltage. This form of gating underlies the generation of nerve and muscle action potentials, among other processes. Here we present the structure of KvAP, a voltage-dependent K+ channel from Aeropyrum pernix. We have determined a crystal structure of the full-length channel at a resolution of 3.2 Å, and of the… 
Electron microscopic analysis of KvAP voltage-dependent K+ channels in an open conformation
TLDR
This finding supports the hypothesis that in response to changes in voltage the sensors move at the protein–lipid interface rather than in a gating pore surrounded by protein.
Voltage Sensor of Kv1.2: Structural Basis of Electromechanical Coupling
TLDR
The x-ray crystal structure of a mammalian Shaker family potassium ion (K+) channel grew three-dimensional crystals, with an internal arrangement that left the voltage sensors in an apparently native conformation, allowing the investigation of the mechanism by which these channels sense cell membrane voltage.
X-ray crystal structure of voltage-gated proton channel
TLDR
A crystal structure of mouse Hv1 in the resting state showing a 'closed umbrella' shape with a long helix consisting of the cytoplasmic coiled coil and the voltage-sensing helix, S4, and featured a wide inner-accessible vestibule provides a platform for understanding the general principles of voltage sensing and proton permeation.
The principle of gating charge movement in a voltage-dependent K+ channel
TLDR
It is concluded that the voltage-sensor paddles operate somewhat like hydrophobic cations attached to levers, enabling the membrane electric field to open and close the pore.
Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane
TLDR
Two structures of the voltage-dependent K+ channel KvAP are presented, in complex with monoclonal Fv fragments and without antibody fragments, and the model is consistent with the proposal of voltage sensing through the movement of an arginine-containing helix-turn-helix element at the protein-lipid interface.
Multiple modes of a-type potassium current regulation.
TLDR
The biophysical and physiological properties of multiple modes of A-type channel regulation, which can be modulated by means of protein-protein interactions with so-called beta-subunits that control inactivation voltage sensitivity and other properties, are reviewed.
Voltage-Gated K+ Channels
TLDR
This chapter gives an overview on voltage-gated K+ channels and discusses experiments performed on Shaker that are most informative about the structure and voltage-sensing domain.
Voltage sensor conformations in the open and closed states in ROSETTA structural models of K(+) channels.
TLDR
A unified mechanism of voltage-dependent gating for K(v)1.2 and KvAP in which this major conformational change moves the gating charge across the electric field in an analogous way for both channels is proposed.
New Structures and Gating of Voltage-Dependent Potassium (Kv) Channels and Their Relatives: A Multi-Domain and Dynamic Question
TLDR
This review considers several aspects of the VSD–PD coupling in Kv channels, and in some relatives, that share a common general structure characterized by a single square-shaped ion conduction pore in the center, surrounded by four VSDs located at the periphery.
Voltage sensor ring in a native structure of a membrane-embedded potassium channel
Voltage-gated ion channels support electrochemical activity in cells and are largely responsible for information flow throughout the nervous systems. The voltage sensor domains in these channels
...
...

References

SHOWING 1-10 OF 49 REFERENCES
The principle of gating charge movement in a voltage-dependent K+ channel
TLDR
It is concluded that the voltage-sensor paddles operate somewhat like hydrophobic cations attached to levers, enabling the membrane electric field to open and close the pore.
Crystal structure and mechanism of a calcium-gated potassium channel
TLDR
This work has cloned, expressed, analysed electrical properties, and determined the crystal structure of a K+ channel (MthK) from Methanobacterium thermoautotrophicum in the Ca2+-bound, opened state.
The voltage sensor in voltage-dependent ion channels.
TLDR
The theoretical basis of the energy coupling between the electric field and the voltage is presented, which allows the interpretation of the gating charge that moves in one channel, and the novel results on lanthanide-based resonance energy transfer that show small distance changes between residues in the channel molecule.
Functional analysis of an archaebacterial voltage-dependent K+ channel
TLDR
The functional characterization of a voltage-dependent K+ (KV) channel from a hyperthermophilic archaebacterium from an oceanic thermal vent is presented and it is shown that this channel possesses all the functional attributes of classical neuronal KV channels.
The structure of the potassium channel: molecular basis of K+ conduction and selectivity.
TLDR
The architecture of the pore establishes the physical principles underlying selective K+ conduction, which promotes ion conduction by exploiting electrostatic repulsive forces to overcome attractive forces between K+ ions and the selectivity filter.
Voltage Sensor Movements
TLDR
These studies revealed that the four most extracellularly located basic residues of the S4 segment (R362, R365, R368, and R371) and the most intracellular acidic residue in the S2 segment (E293) are the major contributors to the gating charge movement.
Measurement of the movement of the S4 segment during the activation of a voltage-gated potassium channel
TLDR
The data suggest that depolarisation must have caused the S4 segment to move out of the lipid bilayer into the extracellular phase rendering the residues at positions 358, 361, 363 and 366 susceptible to PCMBS attack.
Identification of a translocated protein segment in a voltage-dependent channel
TLDR
This work uses site-directed biotinylation to create conformation-sensitive sites on col-icin la, a bacteriocidal protein that forms a voltage-sensitive mem-brane channel that can be monitored by electrophysiological methods.
Single Streptomyces lividans K+ Channels: Functional Asymmetries and Sidedness of Proton Activation
TLDR
Results demonstrate unambiguously that the protonation sites linked to gating are on the intracellular portion of the KcsA protein.
...
...