PDBsum entry 2ya6

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
470 a.a.
DAN ×2
FMT ×5
_CL ×2
Waters ×585
PDB id:
Name: Hydrolase
Title: Crystal structure of streptococcus pneumoniae nana (tigr4) in complex with dana
Structure: Neuraminidase a. Chain: a, b. Fragment: catalytic domain, residues 280-754. Synonym: nana. Engineered: yes. Other_details: the sequence numbering above corresponds to closest uniprot sequence match unp b2djd9. The sequence nu for the entry should be 303-777
Source: Streptococcus pneumoniae. Organism_taxid: 170187. Strain: tigr4. Expressed in: escherichia coli. Expression_system_taxid: 511693.
2.00Å     R-factor:   0.196     R-free:   0.237
Authors: H.Gut,G.Xu,G.L.Taylor,M.A.Walsh
Key ref: H.Gut et al. (2011). Structural basis for Streptococcus pneumoniae NanA inhibition by influenza antivirals zanamivir and oseltamivir carboxylate. J Mol Biol, 409, 496-503. PubMed id: 21514303 DOI: 10.1016/j.jmb.2011.04.016
18-Feb-11     Release date:   27-Apr-11    
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Protein chains
Pfam   ArchSchema ?
P62575  (NANA_STRPN) -  Sialidase A
1035 a.a.
470 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - Exo-alpha-sialidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)-glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     exo-alpha-sialidase activity     1 term  


DOI no: 10.1016/j.jmb.2011.04.016 J Mol Biol 409:496-503 (2011)
PubMed id: 21514303  
Structural basis for Streptococcus pneumoniae NanA inhibition by influenza antivirals zanamivir and oseltamivir carboxylate.
H.Gut, G.Xu, G.L.Taylor, M.A.Walsh.
The human pathogen Streptococcus pneumoniae is the major cause of bacterial meningitis, respiratory tract infection, septicemia, and otitis media. The bacterium expresses neuraminidase (NA) proteins that contribute to pathogenesis by cleaving sialic acids from host glycoconjugates, thereby enhancing biofilm formation and colonization. Recent in vivo experiments have shown that antiviral compounds, widely used in clinics and designed to inhibit influenza NA, significantly reduce biofilm formation and nasopharyngeal colonization of S. pneumoniae in mice. Here, we present the structural basis for the beneficial effect of these compounds against pneumococcal infection. Crystal structures of pneumococcal NanA in complex with zanamivir and oseltamivir carboxylate are discussed, correlated with measured inhibitory constants K(i), and compared with the binding modes of the inhibitors in the viral enzyme. Inhibitor structures show for the first time how clinically approved anti-influenza compounds interact with an NA of the human pathogen S. pneumoniae and give a rational explanation for their antibacterial effects.