› 6ghz

X-ray diffraction
2.33Å resolution

Structure of Lytic Transglycosylase MltE mutant Y192F from E.coli

Released:
DOI: 10.2210/pdb6ghz/pdb
PDB entry 6ghz coloured by chain, front view.
PDB entry 6ghz coloured by chain, side view.
PDB entry 6ghz coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
A Structural Dissection of the Active Site of the Lytic Transglycosylase MltE from Escherichia coli.
Dik DA, Batuecas MT, Lee M, Mahasenan KV, Marous DR, Lastochkin E, Fisher JF, Hermoso JA, Mobashery S
Biochemistry 57 6090-6098 (2018)
PMID: 30256085

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
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

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Citations

1 review citation

Constructing and deconstructing the bacterial cell wall.
Fisher et al. (2020)

13 mentions without citation

Information Metamaterial Systems.
Cui et al. (2020)
12 more