› 1qut

X-ray diffraction
2.44Å resolution

THE SOLUBLE LYTIC TRANSGLYCOSYLASE SLT35 FROM ESCHERICHIA COLI IN COMPLEX WITH N-ACETYLGLUCOSAMINE

Released:
DOI: 10.2210/pdb1qut/pdb
PDB entry 1qut coloured by chain, front view.
PDB entry 1qut coloured by chain, side view.
PDB entry 1qut coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand.
van Asselt EJ, Dijkstra AJ, Kalk KH, Takacs B, Keck W, Dijkstra BW
Structure 7 1167-80 (1999)
PMID: 10545329

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154236 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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

2 bound ligands:
Ligand NAG 1 x NAG
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P212121
Unit cell:
a: 58.33Å b: 67.848Å c: 98.629Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.191 0.256
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Bacterial peptidoglycan (murein) hydrolases.
Vollmer et al. (2008)
9 more

4 mentions without citation

Viral calciomics: interplays between Ca2+ and virus.
Zhou et al. (2009)
3 more