5V8E
Structure of Bacillus cereus PatB1
Summary for 5V8E
| Entry DOI | 10.2210/pdb5v8e/pdb |
| Related | 5V8D |
| Descriptor | Bacillus cereus PatB1, CITRIC ACID, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | acetyltransferase, cell wall, sgnh hydrolase-like, transferase, unknown function |
| Biological source | Bacillus cereus (strain ATCC 10987 / NRS 248) |
| Total number of polymer chains | 2 |
| Total formula weight | 72529.81 |
| Authors | Sychantha, D.,Little, D.J.,Chapman, R.N.,Boons, G.J.,Robinson, H.,Howell, P.L.,Clarke, A.J. (deposition date: 2017-03-21, release date: 2017-10-18, Last modification date: 2024-10-23) |
| Primary citation | Sychantha, D.,Little, D.J.,Chapman, R.N.,Boons, G.J.,Robinson, H.,Howell, P.L.,Clarke, A.J. PatB1 is an O-acetyltransferase that decorates secondary cell wall polysaccharides. Nat. Chem. Biol., 14:79-85, 2018 Cited by PubMed Abstract: O-Acetylation of the secondary cell wall polysaccharides (SCWP) of the Bacillus cereus group of pathogens, which includes Bacillus anthracis, is essential for the proper attachment of surface-layer (S-layer) proteins to their cell walls. Using a variety of pseudosubstrates and a chemically synthesized analog of SCWP, we report here the identification of PatB1 as a SCWP O-acetyltransferase in Bacillus cereus. Additionally, we report the crystal structure of PatB1, which provides detailed insights into the mechanism of this enzyme and defines a novel subfamily of the SGNH family of esterases and lipases. We propose a model for the O-acetylation of SCWP requiring the translocation of acetyl groups from a cytoplasmic source across the plasma membrane by PatA1 and PatA2 for their transfer to SCWP by PatB1. PubMed: 29083419DOI: 10.1038/nchembio.2509 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
