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Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis.


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 (?/?)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.

SUBMITTER: Strunk RJ 

PROVIDER: S-EPMC3936449 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature

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Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis.

Strunk Robert J RJ   Piemonte Katrina M KM   Petersen Natasha M NM   Koutsioulis Dimitris D   Bouriotis Vassilis V   Perry Kay K   Cole Kathryn E KE  

Acta crystallographica. Section F, Structural biology communications 20140121 Pt 2


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 reporte  ...[more]

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