Andreou Athena, Giastas Petros, Arnaouteli Sofia, Tzanodaskalaki Mary, Tzartos Socrates J, Bethanis Kostas, Bouriotis Vassilis, Eliopoulos Elias E
Department of Biotechnology, Agricultural University of Athens, Iera Odos 75, 11855 Athens, Greece.
Department of Biology, Enzyme Biotechnology Group, University of Crete, Vasilika Vouton, 70013 Heraklion, Crete, Greece.
Acta Crystallogr F Struct Biol Commun. 2019 Apr 1;75(Pt 4):312-320. doi: 10.1107/S2053230X19001766. Epub 2019 Apr 3.
Ba0331 is a putative polysaccharide deacetylase from Bacillus anthracis, the etiological agent of the disease anthrax, that contributes to adaptation of the bacterium under extreme conditions and to maintenance of the cell shape. In the present study, the crystal structure of Ba0331 was determined at 2.6 Å resolution. The structure consists of two domains: a fibronectin type 3-like (Fn3-like) domain and a NodB catalytic domain. The latter is present in all carbohydrate esterase family 4 enzymes, while a comparative analysis of the Fn3-like domain revealed structural plasticity despite the retention of the conserved Fn3-like domain characteristics.
Ba0331是一种来自炭疽芽孢杆菌(炭疽病的病原体)的假定多糖脱乙酰酶,它有助于细菌在极端条件下的适应以及细胞形态的维持。在本研究中,Ba0331的晶体结构在2.6 Å分辨率下得以确定。该结构由两个结构域组成:一个纤连蛋白3型样(Fn3样)结构域和一个NodB催化结构域。后者存在于所有碳水化合物酯酶家族4的酶中,而对Fn3样结构域的比较分析显示,尽管保留了保守的Fn3样结构域特征,但该结构域仍具有结构可塑性。