8TLB
Crystal structure of the peptidoglycan O-acetyltransferase B (PatB) from Campylobacter jejuni, catalytic domain
Summary for 8TLB
| Entry DOI | 10.2210/pdb8tlb/pdb |
| Descriptor | Peptidoglycan O-acetyltransferase B (PatB), CHLORIDE ION (3 entities in total) |
| Functional Keywords | peptidoglycan, o-acetyltransferase, duf459, sgnh hydrolase, transferase |
| Biological source | Campylobacter jejuni |
| Total number of polymer chains | 1 |
| Total formula weight | 28249.63 |
| Authors | Anderson, A.C.,Malloch, T.,Clarke, A.J. (deposition date: 2023-07-26, release date: 2024-12-18, Last modification date: 2025-07-02) |
| Primary citation | Anderson, A.C.,Schultz, B.J.,Snow, E.D.,Brott, A.S.,Stangherlin, S.,Malloch, T.,London, J.R.,Walker, S.,Clarke, A.J. The mechanism of peptidoglycan O-acetylation in Gram-negative bacteria typifies bacterial MBOAT-SGNH acyltransferases. J.Biol.Chem., 301:108531-108531, 2025 Cited by PubMed Abstract: Bacterial cell envelope polymers are commonly modified with acyl groups that provide fitness advantages. Many polymer acylation pathways involve pairs of membrane-bound O-acyltransferase (MBOAT) and SGNH family proteins. As an example, the MBOAT protein PatA and the SGNH protein PatB are required in Gram-negative bacteria for peptidoglycan O-acetylation. The mechanism for how MBOAT-SGNH transferases move acyl groups from acyl-CoA donors made in the cytoplasm to extracellular polymers is unclear. Using the peptidoglycan O-acetyltransferase proteins PatAB, we explore the mechanism of MBOAT-SGNH pairs. We find that the MBOAT protein PatA catalyzes auto-acetylation of an invariant Tyr residue in its conserved C-terminal hexapeptide motif. We also show that PatB can use a synthetic hexapeptide containing an acetylated tyrosine to donate an acetyl group to a peptidoglycan mimetic. Finally, we report the structure of PatB, finding that it has structural features that shape its activity as an O-acetyltransferase and distinguish it from other SGNH esterases and hydrolases. Taken together, our results support a model for peptidoglycan acylation in which a tyrosine-containing peptide at the MBOAT's C-terminus shuttles an acyl group from the MBOAT active site to the SGNH active site, where it is transferred to peptidoglycan. This model likely applies to other systems containing MBOAT-SGNH pairs, such as those that O-acetylate alginate, cellulose, and secondary cell wall polysaccharides. PubMed: 40280421DOI: 10.1016/j.jbc.2025.108531 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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