4n31

X-ray diffraction
2.2Å resolution

Structure and activity of Streptococcus pyogenes SipA: a signal peptidase homologue essential for pilus polymerisation

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:
homo octamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Signal peptidase I Chains: A, B
Molecule details ›
Chains: A, B
Length: 163 amino acids
Theoretical weight: 18.64 KDa
Source organism: Streptococcus pyogenes
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: R9TES9 (Residues: 1-138; Coverage: 100%)
Sequence domains: Signal peptidase, peptidase S26
Structure domains: Umud Fragment, subunit A

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P6422
Unit cell:
a: 132.811Å b: 132.811Å c: 107.156Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.201 0.229
Expression system: Escherichia coli BL21(DE3)