6ryp

X-ray diffraction
2.3Å resolution

Bacterial membrane enzyme structure by the in meso method at 2.3 A resolution

Released:

Function and Biology Details

Reaction catalysed:
Release of signal peptides from bacterial membrane prolipoproteins including murein prolipoprotein. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral sidechains.
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-179670 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipoprotein signal peptidase Chain: A
Molecule details ›
Chain: A
Length: 187 amino acids
Theoretical weight: 21.23 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6GHN9 (Residues: 1-163; Coverage: 100%)
Gene names: SAR1172, lsp, lspA
Sequence domains: Signal peptidase (SPase) II

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P6122
Unit cell:
a: 54.17Å b: 54.17Å c: 317.54Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.256 0.254 0.281
Expression system: Escherichia coli