› 2xtv

X-ray diffraction
1.7Å resolution

Structure of E.coli rhomboid protease GlpG, active site mutant, S201T, orthorhombic crystal form

Released:
DOI: 10.2210/pdb2xtv/pdb
PDB entry 2xtv coloured by chain, front view.
PDB entry 2xtv coloured by chain, side view.
PDB entry 2xtv coloured by chain, top view.
Source organism: Escherichia coli BL21(DE3)
Primary publication:
Structure of rhomboid protease in a lipid environment.
Vinothkumar KR
J Mol Biol 407 232-47 (2011)
PMID: 21256137

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: 180 amino acids
Theoretical weight: 20.26 KDa
Source organism: Escherichia coli BL21(DE3)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09391 (Residues: 93-272; Coverage: 65%)
Gene names: JW5687, b3424, glpG
Sequence domains: Rhomboid family
Structure domains: Rhomboid-like

Ligands and Environments

1 bound ligand:
Ligand MC3 14 x MC3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 38.63Å b: 58.87Å c: 91.09Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.215
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 review citations

Activity-based profiling of proteases.
Sanman et al. (2014)
14 more

8 mentions without citation

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