› 2xow

X-ray diffraction
2.09Å resolution

Structure of GlpG in complex with a mechanism-based isocoumarin inhibitor

Released:
DOI: 10.2210/pdb2xow/pdb
PDB entry 2xow coloured by chain, front view.
PDB entry 2xow coloured by chain, side view.
PDB entry 2xow coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The structural basis for catalysis and substrate specificity of a rhomboid protease.
Vinothkumar KR, Strisovsky K, Andreeva A, Christova Y, Verhelst S, Freeman M
EMBO J 29 3797-809 (2010)
PMID: 20890268

Function and Biology Details

Reaction catalysed: 
Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140629 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rhomboid protease GlpG Chain: A
Molecule details ›
Chain: A
Length: 179 amino acids
Theoretical weight: 20.21 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09391 (Residues: 92-270; Coverage: 65%)
Gene names: JW5687, b3424, glpG
Sequence domains: Rhomboid family
Structure domains: Rhomboid-like

Ligands and Environments

2 bound ligands:
Ligand ISM 1 x ISM
Ligand BNG 16 x BNG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: R32
Unit cell:
a: 110.69Å b: 110.69Å c: 122.151Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.198 0.243
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

The rhomboid-like superfamily: molecular mechanisms and biological roles.
Freeman M. (2014)
16 more

7 mentions without citation

Structure and mechanism of rhomboid protease.
Ha et al. (2013)
6 more