4FPL

Crystal structure of the NanB sialidase from streptococcus pneumoniae in complex with 2-[(3,4-dichlorobenzyl)ammonio]ethanesulfonate

Summary for 4FPL

• Entry DOI: 10.2210/pdb4fpl/pdb
• Related: 2VW0 2VW1 2VW2 4FOQ 4FOV 4FOW 4FOY 4FP2 4FP3 4FPC 4FPE 4FPF 4FPG 4FPH 4FPJ 4FPK 4FPO 4FPY 4FQ4
• Descriptor: Sialidase B, 2-[(3,4-dichlorobenzyl)amino]ethanesulfonic acid, DIMETHYL SULFOXIDE, ... (4 entities in total)
• Functional Keywords: hydrolase, intramolecular trans-sialidase, glycosidase, drug design, neuraminidase, hydrolase-inhibitor complex, hydrolase/inhibitor
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 78299.44

Authors

Brear, P. (deposition date: 2012-06-22, release date: 2012-10-31, Last modification date: 2024-02-28)

Primary citation

Brear, P.,Telford, J.,Taylor, G.L.,Westwood, N.J.
Synthesis and structural characterisation of selective non-carbohydrate-based inhibitors of bacterial sialidases.
Chembiochem, 13:2374-2383, 2012

PubMed Abstract: 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 β-amino-sulfonic acid family of buffers.

PubMed: 23070966
DOI: 10.1002/cbic.201200433

Experimental method

X-RAY DIFFRACTION (2.1 Å)