› 2nr9

X-ray diffraction
2.2Å resolution

Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae

Released:
DOI: 10.2210/pdb2nr9/pdb
PDB 2nr9 coloured by chain and viewed from the front.
PDB 2nr9 coloured by chain and viewed from the side.
PDB 2nr9 coloured by chain and viewed from the top.
Source organism: Haemophilus influenzae 86-028NP
Primary publication:
The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis.
Lemieux MJ, Fischer SJ, Cherney MM, Bateman KS, James MN
Proc. Natl. Acad. Sci. U.S.A. 104 750-4 (2007)
PMID: 17210913

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 domain:

Structure analysis Details

Assemblies composition:
monomeric
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rhomboid protease GlpG Chain: A
Molecule details ›
Chain: A
Length: 196 amino acids
Theoretical weight: 22.14 KDa
Source organism: Haemophilus influenzae 86-028NP
Expression system: Escherichia coli
UniProt:
  • Canonical: P44783 (Residues: 1-192; Coverage: 100%)
Gene names: HI_0618, glpG
Sequence domains: Rhomboid family
Structure domains: Rhomboid-like

Ligands and Environments

2 bound ligands:
Ligand PA6 3 x PA6
Ligand PQE 2 x PQE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 121.288Å b: 35.047Å c: 52.931Å
α: 90° β: 104.02° γ: 90°
R-values:
R R work R free
0.236 0.233 0.295
Expression system: Escherichia coli

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Citations

39 review citations

Substrate-Enzyme Interactions in Intramembrane Proteolysis: γ-Secretase as the Prototype.
Liu et al. (2020)
38 more

19 mentions without citation

Taking the plunge: integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysis.
Urban S. (2010)
18 more