Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis
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 2.0Å 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. © 2014 International Union of Crystallography All rights reserved.
Acta Crystallographica Section F:Structural Biology Communications
Strunk, Robert J.; Piemonte, Katrina M.; Petersen, Natasha M.; Koutsioulis, Dimitris; Bouriotis, Vassilis; Perry, Kay; and Cole, Kathryn E., "Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis" (2014). Faculty Articles Indexed in Scopus. 948.