› 4njp

X-ray diffraction
2.4Å resolution

Proteolysis inside the membrane is a rate-governed reaction not Driven by substrate affinity

Released:
DOI: 10.2210/pdb4njp/pdb
PDB entry 4njp coloured by chain, front view.
PDB entry 4njp coloured by chain, side view.
PDB entry 4njp coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Proteolysis inside the membrane is a rate-governed reaction not driven by substrate affinity.
Dickey SW, Baker RP, Cho S, Urban S
Cell 155 1270-81 (2013)
PMID: 24315097

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 dimer
homo trimer
homo hexamer
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: 23.82 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: R32
Unit cell:
a: 110.62Å b: 110.62Å c: 127.73Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.187 0.244
Expression system: Escherichia coli

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Citations

15 review citations

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