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PDBsum entry 2ya5

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Hydrolase PDB id
2ya5
Jmol
Contents
Protein chains
471 a.a.
Ligands
SIA ×2
FMT ×5
Metals
_CL ×2
Waters ×542

References listed in PDB file
Key reference
Title Structural basis for streptococcus pneumoniae nana inhibition by influenza antivirals zanamivir and oseltamivir carboxylate.
Authors H.Gut, G.Xu, G.L.Taylor, M.A.Walsh.
Ref. J Mol Biol, 2011, 409, 496-503.
PubMed id 21514303
Abstract
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.
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