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5V8D

Structure of Bacillus cereus PatB1 with sulfonyl adduct

Summary for 5V8D
Entry DOI10.2210/pdb5v8d/pdb
Related5V8E
DescriptorBacillus cereus PatB1, SULFATE ION, ... (4 entities in total)
Functional Keywordsacetyltransferase, cell wall, sgnh hydrolase-like, transferase
Biological sourceBacillus cereus (strain ATCC 10987 / NRS 248)
More
Total number of polymer chains4
Total formula weight169124.88
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 citationSychantha, 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: 29083419
DOI: 10.1038/nchembio.2509
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.001 Å)
Structure validation

226707

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