› 4c2c

X-ray diffraction
1.9Å resolution

Crystal structure of the protease CtpB in an active state

Released:
DOI: 10.2210/pdb4c2c/pdb
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PDB entry 4c2c coloured by chain, front view.
PDB entry 4c2c coloured by chain, side view.
PDB entry 4c2c coloured by chain, top view.
Source organisms:
Primary publication:
CtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation in Bacillus subtilis.
Mastny M, Heuck A, Kurzbauer R, Heiduk A, Boisguerin P, Volkmer R, Ehrmann M, Rodrigues CD, Rudner DZ, Clausen T
OpenAccess logo Cell 155 647-58 (2013)
PMID: 24243021

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.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128635 (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: 50.26 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

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 11 x MSE

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P3221
Unit cell:
a: 118.785Å b: 118.785Å c: 72.66Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 0.216
Expression system: Escherichia coli BL21

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Citations

4 review citations

Protein Defense Systems against the Lantibiotic Nisin: Function of the Immunity Protein NisI and the Resistance Protein NSR.
Khosa et al. (2016)
3 more

3 mentions without citation

Discovery of Novel µ-Opioid Receptor Inverse Agonist from a Combinatorial Library of Tetrapeptides through Structure-Based Virtual Screening.
Poli et al. (2019)
2 more

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