Publication Abstract from PubMed
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 A resolution. The overall structure maintains the conserved (alpha/beta)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.
Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis.,Strunk RJ, Piemonte KM, Petersen NM, Koutsioulis D, Bouriotis V, Perry K, Cole KE Acta Crystallogr F Struct Biol Commun. 2014 Feb;70(Pt 2):156-9. doi:, 10.1107/S2053230X13034262. Epub 2014 Jan 21. PMID:24637747[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
