9VKI
Oligosaccharide sulfotransferase
Summary for 9VKI
| Entry DOI | 10.2210/pdb9vki/pdb |
| Descriptor | LPS sulfotransferase NodH (1 entity in total) |
| Functional Keywords | oligosaccharide sulfotransferase, sugar binding protein |
| Biological source | Saccharothrix tamanrassetensis |
| Total number of polymer chains | 2 |
| Total formula weight | 59655.04 |
| Authors | |
| Primary citation | Cao, Y.,Guo, S.,Piao, Y.,Zhang, W.,Sun, P.,Cui, L.,Deng, Z.,Zhang, Q.,Ding, W. Sulfation in the Biosynthesis of the Heptadecaglycoside Antibiotic Saccharomicin A. Jacs Au, 6:3405-3413, 2026 Cited by PubMed Abstract: Sulfation is a ubiquitous modification in glycobiology, yet its enzymology and biological significance in glycosylated natural products remain poorly understood. Saccharomicin A, a potent oligosaccharide antibiotic, carries 17 sugars including a unique sulfated fucose. Here, we report the identification of Sam10 as an unprecedented fucose-specific sulfotransferase through genetic studies, reconstitution, and structural analysis, establishing its role in saccharomicin sulfation. Comparative bioassays revealed that sulfation contributes to antibacterial potency, including activity against diverse multidrug-resistant pathogens. We also characterized Sam35 as an efficient adenylyl-sulfate kinase that boosts cellular 3'-phosphoadenosine-5'-phosphate sulfate (PAPS) supply. Our findings define the biochemical and structural basis of saccharomicin sulfation and provide enzymatic tools for engineering novel sulfated oligosaccharide antibiotics. PubMed: 42358689DOI: 10.1021/jacsau.6c00414 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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