2ae0

X-ray diffraction
2Å resolution

Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold

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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Membrane-bound lytic murein transglycosylase A Chain: X
Molecule details ›
Chain: X
Length: 345 amino acids
Theoretical weight: 38.25 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A935 (Residues: 22-365; Coverage: 100%)
Gene names: JW2784, b2813, mlt, mltA, ygdM
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P3121
Unit cell:
a: 103.873Å b: 103.873Å c: 109.777Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.203 0.237
Expression system: Escherichia coli