4m1b | pdb_00004m1b
From Proteopedia
Structural Determination of BA0150, a Polysaccharide Deacetylase from Bacillus anthracis
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Structural highlights
FunctionPublication Abstract from PubMedPolysaccharide 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. References
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This page was last modified 10:46, 21 December 2022.