4M1B: Structural Determination Of Ba0150, A Polysaccharide Deacetylase From Bacillus Anthracis

Citation:
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 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.
PDB ID: 4M1BDownload
MMDB ID: 117492
PDB Deposition Date: 2013/8/2
Updated in MMDB: 2014/10
Experimental Method:
x-ray diffraction
Resolution: 1.99  Å
Source Organism:
Similar Structures:
Biological Unit for 4M1B: monomeric; determined by author and by software (PISA)
Molecular Components in 4M1B
Label Count Molecule
Protein (1 molecule)
1
Polysaccharide Deacetylase
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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