ArticleBiochemistry2012
Structural studies of the spinosyn rhamnosyltransferase, SpnG.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- Enhancement of spinosad production in Saccharopolyspora spinosa by overexpression of the complete 74-kb spinosyn gene cluster.Microbial cell factories · 2025Article
- Review
- Preference of Bacterial Rhamnosyltransferases for 6-Deoxysugars Reveals a Strategy To Deplete O-Antigens.Journal of the American Chemical Society · 2023Article
- Rethinking Biosynthesis of Aclacinomycin A.Molecules (Basel, Switzerland) · 2023Review
- Improving spinosad production by tuning expressions of the forosamine methyltransferase and the forosaminyl transferase to reduce undesired less active byproducts in the heterologous host Streptomyces albus J1074.Microbial cell factories · 2023Article
- Rhamnose-Containing Compounds: Biosynthesis and Applications.Molecules (Basel, Switzerland) · 2022Review
- Biochemical characterization of a glycosyltransferase Gtf3 from3 Biotech · 2020Article
- Structural basis of protein arginine rhamnosylation by glycosyltransferase EarP.Nature chemical biology · 2018Article
- Structural characterization of O- and C-glycosylating variants of the landomycin glycosyltransferase LanGT2.Angewandte Chemie (International ed. in English) · 2015Article
- Computational study of a model system of enzyme-mediated [4+2] cycloaddition reaction.PloS one · 2015Article
- Chemoenzymatic synthesis of spinosyn A.Angewandte Chemie (International ed. in English) · 2014Article
- Structural studies of the spinosyn forosaminyltransferase, SpnP.Biochemistry · 2014Article
- Crystal structure of SsfS6, the putative C-glycosyltransferase involved in SF2575 biosynthesis.Proteins · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Spinosyns A and D (spinosad), like many other complex polyketides, are tailored near the end of their biosyntheses through the addition of sugars. SpnG, which catalyzes their 9-OH rhamnosylation, is also capable of adding other monosaccharides to the spinosyn aglycone (AGL) from TDP-sugars; however, the substitution of UDP-D-glucose for TDP-D-glucose as the donor substrate is known to result in a >60000-fold reduction in k(cat). Here, we report the structure of SpnG at 1.65 Å resolution, SpnG bound to TDP at 1.86 Å resolution, and SpnG bound to AGL at 1.70 Å resolution. The SpnG-TDP complex reveals how SpnG employs N202 to discriminate between TDP- and UDP-sugars. A conformational change of several residues in the active site is promoted by the binding of TDP. The SpnG-AGL complex shows that the binding of AGL is mediated via hydrophobic interactions and that H13, the potential catalytic base, is within 3 Å of the nucleophilic 9-OH group of AGL. A model for the Michaelis complex was constructed to reveal the features that allow SpnG to transfer diverse sugars; it also revealed that the rhamnosyl moiety is in a skew-boat conformation during the transfer reaction.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.