2pi8

X-ray diffraction
2.25Å resolution

Crystal structure of E. coli MltA with bound chitohexaose

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.

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Membrane-bound lytic murein transglycosylase A Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 345 amino acids
Theoretical weight: 38.63 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0A935 (Residues: 22-365; Coverage: 100%)
Gene names: JW2784, b2813, mlt, mltA, ygdM
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1, EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P31
Unit cell:
a: 91Å b: 91Å c: 187.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.182 0.226
Expression system: Escherichia coli BL21