1LNQ

CRYSTAL STRUCTURE OF MTHK AT 3.3 A

1LNQ の概要

• エントリーDOI: 10.2210/pdb1lnq/pdb
• 分子名称: POTASSIUM CHANNEL RELATED PROTEIN, CALCIUM ION (2 entities in total)
• 機能のキーワード: rossmann fold, helix bundle, membrane protein, metal transport
• 由来する生物種: Methanothermobacter thermautotrophicus
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: O27564
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 299169.90

構造登録者

Jiang, Y.,Lee, A.,Chen, J.,Cadene, M.,Chait, B.T.,Mackinnon, R. (登録日: 2002-05-03, 公開日: 2002-06-19, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.3 Å)