4V33

Crystal structure of the putative polysaccharide deacetylase BA0330 from bacillus anthracis

Summary for 4V33

• Entry DOI: 10.2210/pdb4v33/pdb
• Descriptor: POLYSACCHARIDE DEACETYLASE-LIKE PROTEIN, ACETATE ION, ZINC ION, ... (5 entities in total)
• Functional Keywords: hydrolase, fibronectin type iii domain
• Biological source: BACILLUS ANTHRACIS
• Total number of polymer chains: 2
• Total formula weight: 82351.99

Authors

Giastas, P.,Andreou, A.,Bouriotis, V.,Eliopoulos, E. (deposition date: 2014-10-16, release date: 2015-04-08, Last modification date: 2024-01-10)

Primary citation

Arnaouteli, S.,Giastas, P.,Andreou, A.,Tzanodaskalaki, M.,Aldridge, C.,Tzartos, S.J.,Vollmer, W.,Eliopoulos, E.,Bouriotis, V.
Two Putative Polysaccharide Deacetylases are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus Anthracis.
J.Biol.Chem., 290:13465-, 2015

PubMed 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) β-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.

PubMed: 25825488
DOI: 10.1074/JBC.M115.640029

Experimental method

X-RAY DIFFRACTION (1.48 Å)