› 1jtn

X-ray diffraction
2.3Å resolution

Alternative Structures of a Sequence Extended T4 Lysozyme Show that the Highly Conserved Beta-Sheet Region has weak intrinsic Folding Propensity

Released:
DOI: 10.2210/pdb1jtn/pdb
PDB entry 1jtn coloured by chain, front view.
PDB entry 1jtn coloured by chain, side view.
PDB entry 1jtn coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Crystal structures of a T4-lysozyme duplication-extension mutant demonstrate that the highly conserved beta-sheet region has low intrinsic folding propensity.
Sagermann M, Matthews BW
J Mol Biol 316 931-40 (2002)
PMID: 11884133

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 178 amino acids
Theoretical weight: 20.22 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

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 60.125Å b: 32.314Å c: 85.925Å
α: 90° β: 102.64° γ: 90°
R-values:
R R work R free
0.232 0.22 0.314
Expression system: Escherichia coli

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Citations

4 review citations

Bacteriophage endolysins as novel antimicrobials.
Schmelcher et al. (2012)
3 more