› 1t7d

X-ray diffraction
2.47Å resolution

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

Released:
DOI: 10.2210/pdb1t7d/pdb
PDB entry 1t7d coloured by chain, front view.
PDB entry 1t7d coloured by chain, side view.
PDB entry 1t7d coloured by chain, top view.
Source organisms:
Primary publication:
Crystallographic and biophysical analysis of a bacterial signal peptidase in complex with a lipopeptide-based inhibitor.
Paetzel M, Goodall JJ, Kania M, Dalbey RE, Page MG
J Biol Chem 279 30781-90 (2004)
PMID: 15136583

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133585 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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: Signal peptidase, peptidase S26
Structure domains:
ARYLOMYCIN A2 Chains: C, D
Molecule details ›
Chains: C, D
Length: 6 amino acids
Theoretical weight: 645 Da
Source organism: Streptomyces sp.

Ligands and Environments

1 bound ligand:
Ligand M12 2 x M12
3 modified residues:
Ligand DSE 2 x DSE
Ligand DAL 2 x DAL
Ligand 5PG 2 x 5PG

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)

Quick links

Citations

15 review citations

New antibiotics from bacterial natural products.
Clardy et al. (2006)
14 more

15 mentions without citation

Membrane proteases in the bacterial protein secretion and quality control pathway.
Dalbey et al. (2012)
14 more