› 1l19

X-ray diffraction
1.7Å resolution

ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES

Released:
DOI: 10.2210/pdb1l19/pdb
PDB entry 1l19 coloured by chain, front view.
PDB entry 1l19 coloured by chain, side view.
PDB entry 1l19 coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.
Nicholson H, Becktel WJ, Matthews BW
Nature 336 651-6 (1988)
PMID: 3200317

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: 18.69 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 61.1Å b: 61.1Å c: 97Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.153 not available not available
Expression system: Not provided

Quick links

Citations

13 review citations

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Vieille et al. (2001)
12 more

1 mention without citation

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