› 1kn9

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF A BACTERIAL SIGNAL PEPTIDASE APO-ENZYME, IMPLICATIONS FOR SIGNAL PEPTIDE BINDING AND THE SER-LYS DYAD MECHANISM.

Released:
DOI: 10.2210/pdb1kn9/pdb
PDB entry 1kn9 coloured by chain, front view.
PDB entry 1kn9 coloured by chain, side view.
PDB entry 1kn9 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanism.
Paetzel M, Dalbey RE, Strynadka NC
J Biol Chem 277 9512-9 (2002)
PMID: 11741964

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133584 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Signal peptidase I Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 249 amino acids
Theoretical weight: 27.97 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00803 (Residues: 76-324; Coverage: 77%)
Gene names: JW2552, b2568, lepB
Sequence domains: Signal peptidase, peptidase S26
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P41212
Unit cell:
a: 112.441Å b: 112.441Å c: 198.675Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.239 0.278
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 review citations

Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration.
Ekici et al. (2008)
14 more

12 mentions without citation

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