› 3iiq

X-ray diffraction
2Å resolution

Crystallographic analysis of bacterial signal peptidase in ternary complex with Arylomycin A2 and a beta-sultam inhibitor

Released:
DOI: 10.2210/pdb3iiq/pdb
PDB entry 3iiq coloured by chain, front view.
PDB entry 3iiq coloured by chain, side view.
PDB entry 3iiq coloured by chain, top view.
Source organisms:
Primary publication:
Crystallographic analysis of bacterial signal peptidase in ternary complex with arylomycin A2 and a beta-sultam inhibitor.
Luo C, Roussel P, Dreier J, Page MG, Paetzel M
Biochemistry 48 8976-84 (2009)
PMID: 19655811

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 analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133586 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Signal peptidase I Chains: A, B
Molecule details ›
Chains: A, B
Length: 249 amino acids
Theoretical weight: 27.97 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P00803 (Residues: 76-324; 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

5 bound ligands:
Ligand JZA 2 x JZA
Ligand TRT 2 x TRT
Ligand GOL 4 x GOL
Ligand CCN 2 x CCN
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: ALS BEAMLINE 8.2.2
Spacegroup: P43212
Unit cell:
a: 70.007Å b: 70.007Å c: 259.894Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.207 0.25
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

5 mentions without citation

Signal peptidase I: cleaving the way to mature proteins.
Auclair et al. (2012)
4 more