1ORS

X-ray structure of the KvAP potassium channel voltage sensor in complex with an Fab

Summary for 1ORS

• Entry DOI: 10.2210/pdb1ors/pdb
• Related: 1ORQ
• Descriptor: 33H1 Fab light chain, 33H1 Fab heavy chain, potassium channel, ... (4 entities in total)
• Functional Keywords: potassium channel, voltage-dependent, voltage sensor, kvap, fab complex, membrane protein
• Biological source: Aeropyrum pernix; More
• Cellular location: Cell membrane; Single-pass membrane protein (Potential): P01869; Cell membrane; Multi-pass membrane protein: Q9YDF8
• Total number of polymer chains: 3
• Total formula weight: 62083.06

Authors

Jiang, Y.,Lee, A.,Chen, J.,Ruta, V.,Cadene, M.,Chait, B.T.,MacKinnon, R. (deposition date: 2003-03-14, release date: 2003-05-06, Last modification date: 2024-10-30)

Primary citation

Jiang, Y.,Lee, A.,Chen, J.,Ruta, V.,Cadene, M.,Chait, B.T.,MacKinnon, R.
X-ray structure of a voltage-dependent K+ channel
Nature, 423:33-41, 2003

PubMed Abstract: 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 A, and of the isolated voltage-sensor domain at 1.9 A, both in complex with monoclonal Fab fragments. The channel contains a central ion-conduction pore surrounded by voltage sensors, which form what we call 'voltage-sensor paddles'-hydrophobic, cationic, helix-turn-helix structures on the channel's outer perimeter. Flexible hinges suggest that the voltage-sensor paddles move in response to membrane voltage changes, carrying their positive charge across the membrane.

PubMed: 12721618
DOI: 10.1038/nature01580

Experimental method

X-RAY DIFFRACTION (1.9 Å)