6ghz

X-ray diffraction
2.33Å resolution

Structure of Lytic Transglycosylase MltE mutant Y192F from E.coli

Released:

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-type membrane-bound lytic murein transglycosylase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 194 amino acids
Theoretical weight: 21.4 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C960 (Residues: 19-203; Coverage: 98%)
Gene names: JW5821, b1193, emtA, mltE, sltZ, ycgP
Sequence domains: Transglycosylase SLT domain
Structure domains: Lysozyme

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: C2221
Unit cell:
a: 120.028Å b: 181.339Å c: 35.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.234 0.304
Expression system: Escherichia coli