Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis.
Publication Type:Journal Article
Source:Acta Crystallogr F Struct Biol Commun, Volume 70, Issue Pt 2, p.156-9 (2014)
Keywords:Amidohydrolases, Amino Acid Sequence, Bacillus anthracis, Crystallography, X-Ray, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid, Spectrometry, X-Ray Emission
<p>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.</p>