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Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis
Author(s) -
Strunk Robert J.,
Piemonte Katrina M.,
Petersen Natasha M.,
Koutsioulis Dimitris,
Bouriotis Vassilis,
Perry Kay,
Cole Kathryn E.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x13034262
Subject(s) - bacillus anthracis , enzyme , biochemistry , acetylation , bacteria , microbiology and biotechnology , transferase , chemistry , polysaccharide , bacillus (shape) , biology , gene , genetics
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.