› 1w8o

X-ray diffraction
1.7Å resolution

Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens

Released:
DOI: 10.2210/pdb1w8o/pdb
PDB entry 1w8o coloured by chain, front view.
PDB entry 1w8o coloured by chain, side view.
PDB entry 1w8o coloured by chain, top view.
Source organism: Micromonospora viridifaciens
Primary publication:
Contribution of the active site aspartic acid to catalysis in the bacterial neuraminidase from Micromonospora viridifaciens.
Watson JN, Newstead S, Dookhun V, Taylor G, Bennet AJ
FEBS Lett 577 265-9 (2004)
PMID: 15527797

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
Macromolecules (2 distinct):
Sialidase Chain: A
Molecule details ›
Chain: A
Length: 601 amino acids
Theoretical weight: 64.24 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

Carbohydrate polymer : NEW Components: GLC, GAL
Carbohydrate polymer
3 bound ligands:
Ligand CIT 1 x CIT
Ligand GOL 4 x GOL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 46.712Å b: 111.168Å c: 142.195Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.162 0.197
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Features and applications of bacterial sialidases.
Kim et al. (2011)
7 other articles

2 mentions without citation

Sequence and structural analysis of the Asp-box motif and Asp-box beta-propellers; a widespread propeller-type characteristic of the Vps10 domain family and several glycoside hydrolase families.
Quistgaard et al. (2009)
1 more