› 3t36

X-ray diffraction
2.25Å resolution

Crystal structure of lytic transglycosylase MltE from Eschericha coli

Released:
DOI: 10.2210/pdb3t36/pdb
PDB entry 3t36 coloured by chain, front view.
PDB entry 3t36 coloured by chain, side view.
PDB entry 3t36 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
On the mechanism of peptidoglycan binding and cleavage by the endo-specific lytic transglycosylase MltE from Escherichia coli.
Fibriansah G, Gliubich FI, Thunnissen AM
Biochemistry 51 9164-77 (2012)
PMID: 23075328

Function and Biology Details

Reaction catalysed: 
Endolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143188 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-type membrane-bound lytic murein transglycosylase A Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 203 amino acids
Theoretical weight: 22.21 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C960 (Residues: 17-203; Coverage: 100%)
Gene names: JW5821, b1193, emtA, mltE, sltZ, ycgP
Sequence domains: Transglycosylase SLT domain
Structure domains: Lysozyme

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 77.764Å b: 94.925Å c: 160.494Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.189 0.224
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Cell-Wall Recycling of the Gram-Negative Bacteria and the Nexus to Antibiotic Resistance.
Dik et al. (2018)
1 more

4 mentions without citation

Lytic transglycosylases: concinnity in concision of the bacterial cell wall.
Dik et al. (2017)
3 more