PDBsum entry 4fp3

Hydrolase/inhibitor

PDB id: 4fp3

Contents

Protein chain

658 a.a.

Ligands

IJ2

Waters ×172

PDB id:

4fp3

Name:

Hydrolase/inhibitor

Title:

Crystal structure of the nanb sialidase from streptococcus pneumoniae in complex with 2-[(furan-2-ylmethyl)ammonio]sulfonate

Structure:

Sialidase b. Chain: a. Synonym: neuraminidase b. Engineered: yes

Source:

Streptococcus pneumoniae. Organism_taxid: 1313. Strain: tigr4. Gene: nanb, sp_1687. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.74Å R-factor: 0.183 R-free: 0.251

Authors:

P.Brear

Key ref:

P.Brear et al. (2012). Synthesis and structural characterisation of selective non-carbohydrate-based inhibitors of bacterial sialidases. Chembiochem, 13, 2374-2383. PubMed id: 23070966

Date:

21-Jun-12 Release date: 31-Oct-12

Protein chain

Q54727  (NANB_STRPN) -  Sialidase B from Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

Seq: 697 a.a.

Struc: 658 a.a.

Enzyme reactions

• Enzyme class: E.C.3.2.1.18 - exo-alpha-sialidase.
• 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.

Chembiochem 13:2374-2383 (2012)

PubMed id: 23070966

Synthesis and structural characterisation of selective non-carbohydrate-based inhibitors of bacterial sialidases.

P.Brear, J.Telford, G.L.Taylor, N.J.Westwood.

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.