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9VKI

Oligosaccharide sulfotransferase

Summary for 9VKI
Entry DOI10.2210/pdb9vki/pdb
DescriptorLPS sulfotransferase NodH (1 entity in total)
Functional Keywordsoligosaccharide sulfotransferase, sugar binding protein
Biological sourceSaccharothrix tamanrassetensis
Total number of polymer chains2
Total formula weight59655.04
Authors
Cao, Y.,Cao, Y. (deposition date: 2025-06-23, release date: 2026-06-03, Last modification date: 2026-07-08)
Primary citationCao, 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: 42358689
DOI: 10.1021/jacsau.6c00414
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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PDB entries from 2026-08-12

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