4cfp

X-ray diffraction
2.15Å resolution

Crystal structure of MltC in complex with tetrasaccharide at 2.15 A resolution

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

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-142857 (preferred)
Entry contents:
1 distinct polypeptide molecule
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

Ligands and Environments

Carbohydrate polymer : NEW Components: AMV, NAG, AMU
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P21
Unit cell:
a: 49.51Å b: 114.33Å c: 61.771Å
α: 90° β: 93.28° γ: 90°
R-values:
R R work R free
0.195 0.191 0.268
Expression system: Escherichia coli