6iqq

X-ray diffraction
2.8Å resolution

Crystal structure of Prc with S452I and L252Y mutations in complex with NlpI

Released:
Model geometry
Fit model/data

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 orTyr, and Zaa is preferably Ala, but then cleaves at a variable distancefrom 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:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-142703 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lipoprotein NlpI Chains: A, B
Molecule details ›
Chains: A, B
Length: 296 amino acids
Theoretical weight: 33.84 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0AFB1 (Residues: 20-294; Coverage: 100%)
Gene names: JW3132, b3163, nlpI, yhbM
Tail-specific protease Chains: C, D
Molecule details ›
Chains: C, D
Length: 688 amino acids
Theoretical weight: 77.67 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P23865 (Residues: 1-682; Coverage: 100%)
Gene names: JW1819, b1830, prc, tsp
Sequence domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSRRC BEAMLINE TPS 05A
Spacegroup: P212121
Unit cell:
a: 118.936Å b: 143.882Å c: 153.599Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.222 0.278
Expression systems:
  • Escherichia coli BL21
  • Escherichia coli BL21(DE3)