4M1B

Structural Determination of BA0150, a Polysaccharide Deacetylase from Bacillus anthracis

Summary for 4M1B

• Entry DOI: 10.2210/pdb4m1b/pdb
• Descriptor: Polysaccharide deacetylase, TRIETHYLENE GLYCOL (3 entities in total)
• Functional Keywords: polysaccharide deacetylase, carbohydrate esterase, nobb domain, polysaccharide deacetylation, hydrolase
• Biological source: Bacillus anthracis (anthrax,anthrax bacterium)
• Total number of polymer chains: 2
• Total formula weight: 57361.66

Authors

Cole, K.E.,Perry, K. (deposition date: 2013-08-02, release date: 2014-02-12, Last modification date: 2024-02-28)

Primary citation

Strunk, R.J.,Piemonte, K.M.,Petersen, N.M.,Koutsioulis, D.,Bouriotis, V.,Perry, K.,Cole, K.E.
Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis.
Acta Crystallogr F Struct Biol Commun, 70:156-159, 2014

PubMed 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 (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.

PubMed: 24637747
DOI: 10.1107/S2053230X13034262

Experimental method

X-RAY DIFFRACTION (1.99 Å)