› 3ubb

X-ray diffraction
2.6Å resolution

The crystal structure of GlpG in complex with a phosphonofluoridate inhibitor

Released:
DOI: 10.2210/pdb3ubb/pdb
PDB entry 3ubb coloured by chain, front view.
PDB entry 3ubb coloured by chain, side view.
PDB entry 3ubb coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Conformational change in rhomboid protease GlpG induced by inhibitor binding to its S' subsites.
Xue Y, Chowdhury S, Liu X, Akiyama Y, Ellman J, Ha Y
Biochemistry 51 3723-31 (2012)
PMID: 22515733

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

Assemblies composition:
monomeric (preferred)
homo trimer
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: 182 amino acids
Theoretical weight: 20.53 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09391 (Residues: 91-272; Coverage: 66%)
Gene names: JW5687, b3424, glpG
Sequence domains: Rhomboid family
Structure domains: Rhomboid-like

Ligands and Environments

1 bound ligand:
Ligand 3UB 1 x 3UB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: R32
Unit cell:
a: 111.722Å b: 111.722Å c: 121.81Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.212 0.211 0.229
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

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

3 mentions without citation

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