4V33

Crystal structure of the putative polysaccharide deacetylase BA0330 from bacillus anthracis

4V33 の概要

• エントリーDOI: 10.2210/pdb4v33/pdb
• 分子名称: POLYSACCHARIDE DEACETYLASE-LIKE PROTEIN, ACETATE ION, ZINC ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, fibronectin type iii domain
• 由来する生物種: BACILLUS ANTHRACIS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82351.99

構造登録者

Giastas, P.,Andreou, A.,Bouriotis, V.,Eliopoulos, E. (登録日: 2014-10-16, 公開日: 2015-04-08, 最終更新日: 2024-01-10)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.48 Å)