4chx

X-ray diffraction
2.45Å resolution

Crystal structure of MltC in complex with disaccharide pentapeptide DHl89

Released:

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:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
PDBe Complex ID:
PDB-CPX-142858 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Membrane-bound lytic murein transglycosylase C Chains: A, B
Molecule details ›
Chains: A, B
Length: 341 amino acids
Theoretical weight: 38.26 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C066 (Residues: 20-359; Coverage: 99%)
Gene names: JW5481, b2963, mltC, yggZ
Sequence domains:
Structure domains: Lysozyme
NAG-ANHMUR-PENTAPEPTIDE Chain: C
Molecule details ›
Chain: C
Length: 5 amino acids
Theoretical weight: 533 Da
Source organism: synthetic construct

Ligands and Environments

2 bound ligands:
3 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 50.16Å b: 115Å c: 61.28Å
α: 90° β: 93.21° γ: 90°
R-values:
R R work R free
0.196 0.192 0.248
Expression system: Escherichia coli