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X-ray diffraction
1.45Å resolution

T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--Apo structure

Released:
DOI: 10.2210/pdb3gui/pdb
PDB entry 3gui coloured by chain, front view.
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Source organism: Escherichia virus T4
Primary publication:
Use of stabilizing mutations to engineer a charged group within a ligand-binding hydrophobic cavity in T4 lysozyme.
Liu L, Baase WA, Michael MM, Matthews BW
Biochemistry 48 8842-51 (2009)
PMID: 19663503

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133020 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.79 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P00720 (Residues: 1-164; Coverage: 100%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

4 bound ligands:
Ligand BME 1 x BME
Ligand CO3 1 x CO3
Ligand TAM 1 x TAM
Ligand SO4 1 x SO4
1 modified residue:
Ligand CME 2 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P41212
Unit cell:
a: 48.769Å b: 48.769Å c: 128.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.185 0.206
Expression system: Escherichia coli

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Citations

1 review citation

Survey of the year 2009: applications of isothermal titration calorimetry.
Falconer et al. (2011)
14 other articles

2 mentions without citation

Lessons from the lysozyme of phage T4.
Baase et al. (2010)
1 more