3czb

X-ray diffraction
2.5Å resolution

Crystal structure of putative transglycosylase from Caulobacter crescentus

Released:
Source organism: Caulobacter vibrioides CB15
Entry authors: Ramagopal UA, Chattopadhyay K, Toro R, Wasserman S, Freeman J, Logan C, Bain K, Gheyi T, Sauder JM, Burley SK, Almo SC, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Reaction catalysed:
Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-189464 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
peptidoglycan lytic exotransglycosylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 351 amino acids
Theoretical weight: 37.33 KDa
Source organism: Caulobacter vibrioides CB15
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9A226 (Residues: 56-395; Coverage: 91%)
Gene name: CC_3740
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID, APS BEAMLINE 24-ID-C
Spacegroup: P3121
Unit cell:
a: 129.604Å b: 129.604Å c: 88.74Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.199 0.25
Expression system: Escherichia coli