› 1v0e

X-ray diffraction
1.9Å resolution

Endosialidase of Bacteriophage K1F

Released:
DOI: 10.2210/pdb1v0e/pdb
PDB entry 1v0e coloured by chain, front view.
PDB entry 1v0e coloured by chain, side view.
PDB entry 1v0e coloured by chain, top view.
Source organism: Escherichia phage K1F
Primary publication:
Crystal structure of the polysialic acid-degrading endosialidase of bacteriophage K1F.
Stummeyer K, Dickmanns A, Mühlenhoff M, Gerardy-Schahn R, Ficner R
Nat Struct Mol Biol 12 90-6 (2005)
PMID: 15608653

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170081 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mature tail spike protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 666 amino acids
Theoretical weight: 74.13 KDa
Source organism: Escherichia phage K1F
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04830 (Residues: 245-910; Coverage: 63%)
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PO4 6 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P2221
Unit cell:
a: 99.65Å b: 131.25Å c: 346.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.202
Expression system: Escherichia coli

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Citations

27 review citations

Sialic acids in the brain: gangliosides and polysialic acid in nervous system development, stability, disease, and regeneration.
Schnaar et al. (2014)
26 more

8 mentions without citation

Identification of amino acid residues at the active site of endosialidase that dissociate the polysialic acid binding and cleaving activities in Escherichia coli K1 bacteriophages.
Jakobsson et al. (2007)
7 more