› 1wcq

X-ray diffraction
2.1Å resolution

Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine.

Released:
DOI: 10.2210/pdb1wcq/pdb
PDB entry 1wcq coloured by chain, front view.
PDB entry 1wcq coloured by chain, side view.
PDB entry 1wcq coloured by chain, top view.
Source organism: Micromonospora viridifaciens
Primary publication:
Two nucleophilic mutants of the Micromonospora viridifaciens sialidase operate with retention of configuration by two different mechanisms.
Watson JN, Newstead S, Narine AA, Taylor G, Bennet AJ
Chembiochem 6 1999-2004 (2005)
PMID: 16206228

Function and Biology Details

Reaction catalysed: 
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169775 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 601 amino acids
Theoretical weight: 64.28 KDa
Source organism: Micromonospora viridifaciens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q02834 (Residues: 47-647; Coverage: 99%)
Gene name: nedA
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand NA 3 x NA
Ligand GOL 7 x GOL
Ligand DAN 3 x DAN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P3221
Unit cell:
a: 143.258Å b: 143.258Å c: 160.25Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.175 0.238
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Structural insights into sialic acid enzymology.
Buschiazzo et al. (2008)
4 other articles

3 mentions without citation

Identification and characterization of NanH2 and NanH3, enzymes responsible for sialidase activity in the vaginal bacterium Gardnerella vaginalis.
Robinson et al. (2019)
2 more