› 5f5d

X-ray diffraction
2.5Å resolution

Crystal structures and Inhibition kinetics reveal a two-state catalytic mechanism with drug design implications for rhomboid proteolysis

Released:
DOI: 10.2210/pdb5f5d/pdb
PDB entry 5f5d coloured by chain, front view.
PDB entry 5f5d coloured by chain, side view.
PDB entry 5f5d coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal Structures and Inhibition Kinetics Reveal a Two-Stage Catalytic Mechanism with Drug Design Implications for Rhomboid Proteolysis.
Cho S, Dickey SW, Urban S
Mol Cell 61 329-340 (2016)
PMID: 26805573

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: 211 amino acids
Theoretical weight: 23.8 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P09391 (Residues: 87-276; Coverage: 69%)
Gene names: JW5687, b3424, glpG
Sequence domains: Rhomboid family
Structure domains: Rhomboid-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: C2221
Unit cell:
a: 71.185Å b: 98.147Å c: 62.999Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.208 0.284
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Intramembrane proteases as drug targets.
Verhelst SHL. (2017)
6 more

2 mentions without citation

Crystal Structures and Inhibition Kinetics Reveal a Two-Stage Catalytic Mechanism with Drug Design Implications for Rhomboid Proteolysis.
Cho et al. (2016)
1 more