4foy | pdb_00004foy

Crystal structure of the NanB sialidase from streptococcus pneumoniae in complex with 2-(Benzylammonio)ethanesulfonate

spinqualitylabelsall models 4foy, resolution 1.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4foy is a 1 chain structure with sequence from "diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: D53, DMS Related: 2vw0, 2vw1, 2vw2, 4foq, 4fov, 4fow, 4fp2, 4fp3, 4fpc, 4fpe, 4fpf, 4fpg, 4fph, 4fpj, 4fpk, 4fpl, 4fpo, 4fpy, 4fq4 Gene: nanB, SP_1687 ("Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886) Activity: Exo-alpha-sialidase, with EC number 3.2.1.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The major human pathogen Streptococcus pneumoniae plays a key role in several disease states including septicaemia, meningitis and community-acquired pneumonia. Although vaccines against S. pneumoniae are available as prophylactics, there remains a need to identify and characterise novel chemical entities that can treat the diseases caused by this pathogen. S. pneumoniae expresses three sialidases, enzymes that cleave sialic acid from carbohydrate-based surface molecules. Two of these enzymes, NanA and NanB, have been implicated in the pathogenesis of S. pneumoniae and are considered to be validated drug targets. Here we report our studies on the synthesis and structural characterisation of novel NanB-selective inhibitors that are inspired by the beta-amino-sulfonic acid family of buffers. Synthesis and structural characterisation of selective non-carbohydrate-based inhibitors of bacterial sialidases.,Brear P, Telford J, Taylor GL, Westwood NJ Chembiochem. 2012 Nov 5;13(16):2374-83. doi: 10.1002/cbic.201200433. Epub 2012, Oct 15. PMID:23070966 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Neuraminidase

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