PDBe 1t7d

X-ray diffraction
2.47Å resolution

Crystal structure of Escherichia coli type I signal peptidase in complex with a lipopeptide inhibitor

Released:

Function and Biology Details

Reaction catalysed:
Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ARYLOMYCIN A2 Chains: C, D
Molecule details ›
Chains: C, D
Length: 6 amino acids
Theoretical weight: 645 Da
Source organism: Streptomyces sp.
UniProt:
Signal peptidase I Chains: A, B
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 28.08 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00803 (Residues: 75-324; Coverage: 77%)
Gene names: JW2552, b2568, lepB
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

3 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P43212
Unit cell:
a: 69.609Å b: 69.609Å c: 258.466Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.23 0.283
Expression system: Escherichia coli BL21(DE3)