| Literature DB >> 24637747 |
Robert J Strunk1, Katrina M Piemonte1, Natasha M Petersen1, Dimitris Koutsioulis2, Vassilis Bouriotis2, Kay Perry3, Kathryn E Cole1.
Abstract
Polysaccharide deacetylases are bacterial enzymes that catalyze the deacetylation of acetylated sugars on the membranes of Gram-positive bacteria, allowing them to be unrecognized by host immune systems. Inhibition of these enzymes would disrupt such pathogenic defensive mechanisms and therefore offers a promising route for the development of novel antibiotic therapeutics. Here, the first X-ray crystal structure of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis, is reported to 2.0 Å resolution. The overall structure maintains the conserved (α/β)8 fold that is characteristic of this family of enzymes. The lack of a catalytic metal ion and a distinctive metal-binding site, however, suggest that this enzyme is not a functional polysaccharide deacetylase.Entities:
Keywords: Bacillus anthracis; carbohydrate esterases; polysaccharide deacetylases
Mesh:
Substances:
Year: 2014 PMID: 24637747 PMCID: PMC3936449 DOI: 10.1107/S2053230X13034262
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056