› 131l

X-ray diffraction
1.7Å resolution

STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT

Released:
DOI: 10.2210/pdb131l/pdb
PDB entry 131l coloured by chain, front view.
PDB entry 131l coloured by chain, side view.
PDB entry 131l coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent.
Pjura P, Matthews BW
Protein Sci 2 2226-32 (1993)
PMID: 8298466

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 domain:

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: 18.61 KDa
Source organism: Escherichia virus T4
Expression system: Not provided
UniProt:
  • Canonical: P00720 (Residues: 1-164; Coverage: 100%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

2 bound ligands:
Ligand CL 2 x CL
Ligand BME 2 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 60.9Å b: 60.9Å c: 96.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.158 not available not available
Expression system: Not provided

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Citations

1 review citation

Molecular and chemical engineering of bacteriophages for potential medical applications.
Hodyra et al. (2015)
9 other articles

3 mentions without citation

Six Rossmannoid folds, including the Class I aminoacyl-tRNA synthetases, share a partial core with the anti-codon-binding domain of a Class II aminoacyl-tRNA synthetase.
Cammer et al. (2010)
2 more