› 261l

X-ray diffraction
2.5Å resolution

STRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING

Released:
DOI: 10.2210/pdb261l/pdb
PDB entry 261l coloured by chain, front view.
PDB entry 261l coloured by chain, side view.
PDB entry 261l coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding.
Sagermann M, Baase WA, Matthews BW
Proc Natl Acad Sci U S A 96 6078-83 (1999)
PMID: 10339544

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:
  • not assigned
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: 173 amino acids
Theoretical weight: 19.54 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P00720 (Residues: 1-162; Coverage: 99%)
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
X-ray source: CHESS BEAMLINE A1
Spacegroup: P3221
Unit cell:
a: 61.125Å b: 61.125Å c: 97.338Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.17 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Bacteriophage T4 genome.
Miller et al. (2003)
1 more

1 mention without citation

Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding.
Sagermann et al. (1999)