› 1oyu

X-ray diffraction
2.5Å resolution

Long-Distance conformational changes in a protein engineered by modulated sequence duplication

Released:
DOI: 10.2210/pdb1oyu/pdb
PDB entry 1oyu coloured by chain, front view.
PDB entry 1oyu coloured by chain, side view.
PDB entry 1oyu coloured by chain, top view.
Source organism: Tequatrovirus T4
Primary publication:
Long-distance conformational changes in a protein engineered by modulated sequence duplication.
Sagermann M, Gay L, Matthews BW
Proc Natl Acad Sci U S A 100 9191-5 (2003)
PMID: 12869697

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 175 amino acids
Theoretical weight: 19.51 KDa
Source organism: Tequatrovirus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P00720 (Residues: 1-39, 40-164; 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
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P41212
Unit cell:
a: 60.35Å b: 60.35Å c: 213.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.209 0.324
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Protein thermodynamic structure.
Zhao Q. (2009)
8 other articles

1 mention without citation

Long-distance conformational changes in a protein engineered by modulated sequence duplication.
Sagermann et al. (2003)