1d0k

X-ray diffraction
2.02Å resolution

THE ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35 IN COMPLEX WITH TWO MURODIPEPTIDES (GLCNAC-MURNAC-L-ALA-D-GLU)

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
Macromolecules (2 distinct):
Membrane-bound lytic murein transglycosylase B Chain: A
Molecule details ›
Chain: A
Length: 322 amino acids
Theoretical weight: 36.08 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P41052 (Residues: 40-361; Coverage: 94%)
Gene names: JW2671, b2701, mltB
Sequence domains: Transglycosylase SLT domain
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: AMU, NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P212121
Unit cell:
a: 58.379Å b: 67.825Å c: 98.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.165 0.202
Expression system: Escherichia coli