1LNQ

CRYSTAL STRUCTURE OF MTHK AT 3.3 A

Summary for 1LNQ

• Entry DOI: 10.2210/pdb1lnq/pdb
• Descriptor: POTASSIUM CHANNEL RELATED PROTEIN, CALCIUM ION (2 entities in total)
• Functional Keywords: rossmann fold, helix bundle, membrane protein, metal transport
• Biological source: Methanothermobacter thermautotrophicus
• Cellular location: Cell membrane; Multi-pass membrane protein: O27564
• Total number of polymer chains: 8
• Total formula weight: 299169.90

Authors

Jiang, Y.,Lee, A.,Chen, J.,Cadene, M.,Chait, B.T.,Mackinnon, R. (deposition date: 2002-05-03, release date: 2002-06-19, Last modification date: 2024-02-14)

Primary citation

JIANG, Y.,LEE, A.,CHEN, J.,CADENE, M.,CHAIT, B.T.,MACKINNON, R.
CRYSTAL STRUCTURE AND MECHANISM OF A CALCIUM-GATED POTASSIUM CHANNEL
Nature, 417:515-522, 2002

PubMed Abstract: Ion channels exhibit two essential biophysical properties; that is, selective ion conduction, and the ability to gate-open in response to an appropriate stimulus. Two general categories of ion channel gating are defined by the initiating stimulus: ligand binding (neurotransmitter- or second-messenger-gated channels) or membrane voltage (voltage-gated channels). Here we present the structural basis of ligand gating in a K(+) channel that opens in response to intracellular Ca(2+). We have cloned, expressed, analysed electrical properties, and determined the crystal structure of a K(+) channel (MthK) from Methanobacterium thermoautotrophicum in the Ca(2+)-bound, opened state. Eight RCK domains (regulators of K(+) conductance) form a gating ring at the intracellular membrane surface. The gating ring uses the free energy of Ca(2+) binding in a simple manner to perform mechanical work to open the pore.

PubMed: 12037559
DOI: 10.1038/417515a

Experimental method

X-RAY DIFFRACTION (3.3 Å)