4v33
From Proteopedia
Crystal structure of the putative polysaccharide deacetylase BA0330 from bacillus anthracis
Structural highlights
FunctionPublication Abstract from PubMedMembrane-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 anthacis. 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 high concentration of salt, while BA0331 contributes to 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 high 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. Two putative polysaccharide deacetylases are required for osmotic stability and cell shape maintenance in Bacillus anthracis.,Arnaouteli S, Giastas P, Andreou A, Tzanodaskalaki M, Aldridge C, Tzartos SJ, Vollmer W, Eliopoulos E, Bouriotis V J Biol Chem. 2015 Mar 30. pii: jbc.M115.640029. PMID:25825488[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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