6pja

X-ray diffraction
2.6Å resolution

Time-resolved structural snapshot of proteolysis by GlpG inside the membrane

Released:

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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 BL21(DE3)
UniProt:
  • Canonical: P09391 (Residues: 87-276; Coverage: 69%)
Gene names: JW5687, b3424, glpG
Sequence domains: Rhomboid family
Peptide aldehyde inhibitor Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 548 Da
Source organism: Drosophila melanogaster
Expression system: Not provided

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: 71.77Å b: 99.49Å c: 63.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.26 0.26 0.267
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided