› 3tlu

X-ray diffraction
2.85Å resolution

The GLIC pentameric Ligand-Gated Ion Channel Loop2-24' oxidized mutant in a locally-closed conformation (LC1 subtype)

Released:
DOI: 10.2210/pdb3tlu/pdb
PDB 3tlu coloured by chain and viewed from the front.
PDB 3tlu coloured by chain and viewed from the side.
PDB 3tlu coloured by chain and viewed from the top.
Source organism: Gloeobacter violaceus
Primary publication:
A locally closed conformation of a bacterial pentameric proton-gated ion channel.
Prevost MS, Sauguet L, Nury H, Van Renterghem C, Huon C, Poitevin F, Baaden M, Delarue M, Corringer PJ
Nat. Struct. Mol. Biol. 19 642-9 (2012)
PMID: 22580559

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proton-gated ion channel Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 321 amino acids
Theoretical weight: 36.51 KDa
Source organism: Gloeobacter violaceus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7NDN8 (Residues: 44-359; Coverage: 100%)
Gene names: glr4197, glvI
Sequence domains: Neurotransmitter-gated ion-channel ligand binding domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CL 5 x CL
Ligand LMT 1 x LMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2
Unit cell:
a: 177.33Å b: 127.81Å c: 159.09Å
α: 90° β: 100.77° γ: 90°
R-values:
R R work R free
0.204 0.203 0.223
Expression system: Escherichia coli

Quick links

Citations

21 review citations

Druggable Lipid Binding Sites in Pentameric Ligand-Gated Ion Channels and Transient Receptor Potential Channels.
Cheng et al. (2021)
20 more

3 mentions without citation

Propofol binding to the resting state of the gloeobacter violaceus ligand-gated ion channel (GLIC) induces structural changes in the inter- and intrasubunit transmembrane domain (TMD) cavities.
Ghosh et al. (2013)
2 more