4c2f

X-ray diffraction
2.4Å resolution

Crystal structure of the CtpB R168A mutant present in an active conformation

Released:

Function and Biology Details

Reaction catalysed:
The enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala.

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-128636 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Carboxy-terminal processing protease CtpB Chain: A
Molecule details ›
Chain: A
Length: 446 amino acids
Theoretical weight: 50.17 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O35002 (Residues: 43-480; Coverage: 96%)
Gene names: BSU35240, ctpB, yvjB
Sequence domains:
PEPTIDE1 Chain: B
Molecule details ›
Chain: B
Length: 3 amino acids
Theoretical weight: 231 Da
Source organism: Escherichia coli BL21
PEPTIDE2 Chain: C
Molecule details ›
Chain: C
Length: 7 amino acids
Theoretical weight: 532 Da
Source organism: Escherichia coli BL21

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P3221
Unit cell:
a: 117.909Å b: 117.909Å c: 72.048Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.215 0.265
Expression system: Escherichia coli BL21