3b45

X-ray diffraction
1.9Å resolution

Crystal structure of GlpG at 1.9A resolution

Released:
Source organism: Escherichia coli
Primary publication:
The role of L1 loop in the mechanism of rhomboid intramembrane protease GlpG.
J Mol Biol 374 1104-13 (2007)
PMID: 17976648

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:

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: 20.34 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09391 (Residues: 91-270; Coverage: 65%)
Gene names: JW5687, b3424, glpG
Sequence domains: Rhomboid family
Structure domains: Rhomboid-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: R32
Unit cell:
a: 111Å b: 111Å c: 129Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.215 0.228
Expression system: Escherichia coli BL21(DE3)