› 2xzi

X-ray diffraction
1.45Å resolution

THE ASPERGILLUS FUMIGATUS SIALIDASE IS A KDNASE: STRUCTURAL AND MECHANISTIC INSIGHTS

Released:
DOI: 10.2210/pdb2xzi/pdb
PDB entry 2xzi coloured by chain, front view.
PDB entry 2xzi coloured by chain, side view.
PDB entry 2xzi coloured by chain, top view.
Source organism: Aspergillus fumigatus Af293
Primary publication:
The Aspergillus fumigatus sialidase is a 3-deoxy-D-glycero-D-galacto-2-nonulosonic acid hydrolase (KDNase): structural and mechanistic insights.
Telford JC, Yeung JH, Xu G, Kiefel MJ, Watts AG, Hader S, Chan J, Bennet AJ, Moore MM, Taylor GL
J Biol Chem 286 10783-92 (2011)
PMID: 21247893

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175839 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Exo-alpha-sialidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 386 amino acids
Theoretical weight: 42.12 KDa
Source organism: Aspergillus fumigatus Af293
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q4WQS0 (Residues: 21-406; Coverage: 100%)
Gene name: AFUA_4G13800
Sequence domains: BNR repeat-like domain
Structure domains: Neuraminidase

Ligands and Environments

4 bound ligands:
Ligand KDM 4 x KDM
Ligand NA 2 x NA
Ligand GOL 5 x GOL
Ligand NO2 1 x NO2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 75.81Å b: 57.99Å c: 94.83Å
α: 90° β: 100.14° γ: 90°
R-values:
R R work R free
0.18 0.179 0.205
Expression system: Escherichia coli BL21

Quick links

Citations

11 citation in other articles

Leukocyte inflammatory responses provoked by pneumococcal sialidase.
Chang et al. (2012)
10 more

2 mentions without citation

Interface dynamics explain assembly dependency of influenza neuraminidase catalytic activity.
von Grafenstein et al. (2015)
1 more