4V33: Crystal Structure Of The Putative Polysaccharide Deacetylase Ba0330 From Bacillus Anthracis

Citation:
Abstract
Membrane-anchored lipoproteins have a broad range of functions and play key roles in several cellular processes in Gram-positive bacteria. BA0330 and BA0331 are the only lipoproteins among the 11 known or putative polysaccharide deacetylases of Bacillus anthracis. We found that both lipoproteins exhibit unique characteristics. BA0330 and BA0331 interact with peptidoglycan, and BA0330 is important for the adaptation of the bacterium to grow in the presence of a high concentration of salt, whereas BA0331 contributes to the maintenance of a uniform cell shape. They appear not to alter the peptidoglycan structure and do not contribute to lysozyme resistance. The high resolution x-ray structure of BA0330 revealed a C-terminal domain with the typical fold of a carbohydrate esterase 4 and an N-terminal domain unique for this family, composed of a two-layered (4 + 3) beta-sandwich with structural similarity to fibronectin type 3 domains. Our data suggest that BA0330 and BA0331 have a structural role in stabilizing the cell wall of B. anthracis.
PDB ID: 4V33Download
MMDB ID: 128442
PDB Deposition Date: 2014/10/16
Updated in MMDB: 2015/06
Experimental Method:
x-ray diffraction
Resolution: 1.48  Å
Source Organism:
Similar Structures:
Biological Unit for 4V33: monomeric; determined by author and by software (PISA)
Molecular Components in 4V33
Label Count Molecule
Protein (1 molecule)
1
Polysaccharide Deacetylase-like Protein
Molecule annotation
Chemicals (5 molecules)
1
2
2
1
3
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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