8RI6
Beta-galactosidase (LacZ) purified from E. coli.
Summary for 8RI6
| Entry DOI | 10.2210/pdb8ri6/pdb |
| EMDB information | 19181 |
| Descriptor | Beta-galactosidase, MAGNESIUM ION, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | beta-galactosidase, inhibitor, iminosugar, plant pathogenic bacteria., hydrolase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 469967.61 |
| Authors | Hardenbrook, N.J.,Sheng, Y.,Zhang, P. (deposition date: 2023-12-18, release date: 2025-01-01, Last modification date: 2026-03-25) |
| Primary citation | Sanguankiattichai, N.,Chandrasekar, B.,Sheng, Y.,Hardenbrook, N.,Tabak, W.W.A.,Drapal, M.,Kaschani, F.,Grunwald-Gruber, C.,Krahn, D.,Buscaill, P.,Yamamoto, S.,Kato, A.,Nash, R.,Fleet, G.,Strasser, R.,Fraser, P.D.,Kaiser, M.,Zhang, P.,Preston, G.M.,van der Hoorn, R.A.L. Bacterial pathogen deploys the iminosugar glycosyrin to manipulate plant glycobiology. Science, 388:297-303, 2025 Cited by PubMed Abstract: The extracellular space (apoplast) in plants is a key battleground during microbial infections. To avoid recognition, the bacterial model phytopathogen pv. DC3000 produces glycosyrin. Glycosyrin inhibits the plant-secreted β-galactosidase BGAL1, which would otherwise initiate the release of immunogenic peptides from bacterial flagellin. Here, we report the structure, biosynthesis, and multifunctional roles of glycosyrin. High-resolution cryo-electron microscopy and chemical synthesis revealed that glycosyrin is an iminosugar with a five-membered pyrrolidine ring and a hydrated aldehyde that mimics monosaccharides. Glycosyrin biosynthesis was controlled by virulence regulators, and its production is common in bacteria and prevents flagellin recognition and alters the extracellular glycoproteome and metabolome of infected plants. These findings highlight a potentially wider role for glycobiology manipulation by plant pathogens across the plant kingdom. PubMed: 40245141DOI: 10.1126/science.adp2433 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.06 Å) |
Structure validation
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