2VL0

X-ray structure of a pentameric ligand gated ion channel from Erwinia chrysanthemi (ELIC)

2VL0 の概要

• エントリーDOI: 10.2210/pdb2vl0/pdb
• 分子名称: Cys-loop ligand-gated ion channel (1 entity in total)
• 機能のキーワード: pentameric ligand gated ion channel, membrane protein, prokaryotic cys-loop receptor, cation selective channel
• 由来する生物種: Dickeya chrysanthemi (Pectobacterium chrysanthemi)
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 368219.49

構造登録者

Hilf, R.J.C.,Dutzler, R. (登録日: 2008-01-07, 公開日: 2008-03-11, 最終更新日: 2024-05-08)

主引用文献

Hilf, R.J.C.,Dutzler, R.
X-Ray Structure of a Prokaryotic Pentameric Ligand-Gated Ion Channel
Nature, 452:375-, 2008

PubMed Abstract: Pentameric ligand-gated ion channels (pLGICs) are key players in the early events of electrical signal transduction at chemical synapses. The family codes for a structurally conserved scaffold of channel proteins that open in response to the binding of neurotransmitter molecules. All proteins share a pentameric organization of identical or related subunits that consist of an extracellular ligand-binding domain followed by a transmembrane channel domain. The nicotinic acetylcholine receptor (nAChR) is the most thoroughly studied member of the pLGIC family (for recent reviews see refs 1-3). Two sources of structural information provided an architectural framework for the family. The structure of the soluble acetylcholine-binding protein (AChBP) defined the organization of the extracellular domain and revealed the chemical basis of ligand interaction. Electron microscopy studies of the nAChR from Torpedo electric ray have yielded a picture of the full-length protein and have recently led to the interpretation of an electron density map at 4.0 A resolution. Despite the wealth of experimental information, high-resolution structures of any family member have so far not been available. Until recently, the pLGICs were believed to be only expressed in multicellular eukaryotic organisms. The abundance of prokaryotic genome sequences, however, allowed the identification of several homologous proteins in bacterial sources. Here we present the X-ray structure of a prokaryotic pLGIC from the bacterium Erwinia chrysanthemi (ELIC) at 3.3 A resolution. Our study reveals the first structure of a pLGIC at high resolution and provides an important model system for the investigation of the general mechanisms of ion permeation and gating within the family.

PubMed: 18322461
DOI: 10.1038/NATURE06717

実験手法

X-RAY DIFFRACTION (3.3 Å)