6GO1
Crystal Structure of a Bacillus anthracis peptidoglycan deacetylase
Summary for 6GO1
| Entry DOI | 10.2210/pdb6go1/pdb |
| Descriptor | Polysaccharide deacetylase-like protein, ZINC ION, ACETATE ION, ... (6 entities in total) |
| Functional Keywords | peptidoglycan, deacetylase, bacillus anthracis, hydrolase |
| Biological source | Bacillus anthracis |
| Total number of polymer chains | 2 |
| Total formula weight | 74400.08 |
| Authors | Giastas, P.,Andreou, A.,Eliopoulos, E.E. (deposition date: 2018-06-01, release date: 2019-04-10, Last modification date: 2024-01-17) |
| Primary citation | Andreou, A.,Giastas, P.,Arnaouteli, S.,Tzanodaskalaki, M.,Tzartos, S.J.,Bethanis, K.,Bouriotis, V.,Eliopoulos, E.E. The putative polysaccharide deacetylase Ba0331: cloning, expression, crystallization and structure determination. Acta Crystallogr.,Sect.F, 75:312-320, 2019 Cited by PubMed Abstract: 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. PubMed: 30950833DOI: 10.1107/S2053230X19001766 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.59 Å) |
Structure validation
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