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- Title
Diversity of sugar-diphospholipid-utilizing glycosyltransferase families.
- Authors
Meitil, Ida K. S.; Gippert, Garry P.; Barrett, Kristian; Hunt, Cameron J.; Henrissat, Bernard
- Abstract
Peptidoglycan polymerases, enterobacterial common antigen polymerases, O-antigen ligases, and other bacterial polysaccharide polymerases (BP-Pols) are glycosyltransferases (GTs) that build bacterial surface polysaccharides. These integral membrane enzymes share the particularity of using diphospholipid-activated sugars and were previously missing in the carbohydrate-active enzymes database (CAZy; www.cazy.org). While the first three classes formed well-defined families of similar proteins, the sequences of BP-Pols were so diverse that a single family could not be built. To address this, we developed a new clustering method using a combination of a sequence similarity network and hidden Markov model comparisons. Overall, we have defined 17 new GT families including 14 of BP-Pols. We find that the reaction stereochemistry appears to be conserved in each of the defined BP-Pol families, and that the BP-Pols within the families transfer similar sugars even across Gram-negative and Gram-positive bacteria. Comparison of the new GT families reveals three clans of distantly related families, which also conserve the reaction stereochemistry. Glycosyltransferases that build bacterial surface polysaccharides were classified into 17 new CAZy families. A glycan analysis reveals that the enzymes within each family transfer similar sugars even across Gram-negative and Gram-positive bacteria.
- Subjects
BACTERIAL cell surfaces; STEREOCHEMISTRY; GRAM-positive bacteria; FAMILIES; POLYMERASES; GLYCANS
- Publication
Communications Biology, 2024, Vol 7, Issue 1, p1
- ISSN
2399-3642
- Publication type
Article
- DOI
10.1038/s42003-024-05930-2