5V8D
Structure of Bacillus cereus PatB1 with sulfonyl adduct
Summary for 5V8D
Entry DOI | 10.2210/pdb5v8d/pdb |
Related | 5V8E |
Descriptor | Bacillus cereus PatB1, SULFATE ION, ... (4 entities in total) |
Functional Keywords | acetyltransferase, cell wall, sgnh hydrolase-like, transferase |
Biological source | Bacillus cereus (strain ATCC 10987 / NRS 248) More |
Total number of polymer chains | 4 |
Total formula weight | 169124.88 |
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: 2020-01-08) |
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 (2.001 Å) |
Structure validation
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