ArticleJournal of biomolecular NMR2018
Complete assignment of Ala, Ile, Leu, Met and Val methyl groups of human blood group A and B glycosyltransferases using lanthanide-induced pseudocontact shifts and methyl-methyl NOESY.
Article in Journal of biomolecular NMR, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- AMIGO - Guided assignment ofJournal of biomolecular NMR · 2026Article
- An NMR look at an engineered PET depolymerase.Biophysical journal · 2022Article
- Ligand-induced structural transitions combined with paramagnetic ions facilitate unambiguous NMR assignments of methyl groups in large proteins.Journal of biomolecular NMR · 2022Article
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- Assignment of Ala, Ile, LeuBiomolecular NMR assignments · 2022Article
- Sparse isotope labeling for nuclear magnetic resonance (NMR) of glycoproteins using 13C-glucose.Glycobiology · 2021Article
- Insights into Allosteric Control of Human Blood Group A and B Glycosyltransferases from Dynamic NMR.ChemistryOpen · 2019Article
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Authors and funding
2 authors.
Funding
Abstract
Human blood group A and B glycosyltransferases (GTA, GTB) are highly homologous glycosyltransferases. A number of high-resolution crystal structures is available showing that these enzymes convert from an open conformation into a catalytically active closed conformation upon substrate binding. However, the mechanism of glycosyltransfer is still under debate, and the precise nature as well as the time scales of conformational transitions are unknown. NMR offers a variety of experiments to shine more light on these unresolved questions. Therefore, in a first step we have assigned all methyl resonance signals in MILVA labeled samples of GTA and GTB, still a challenging task for 70 kDa homodimeric proteins. Assignments were obtained from methyl-methyl NOESY experiments, and from measurements of lanthanide-induced pseudocontact shifts (PCS) using high resolution crystal structures as templates. PCSs and chemical shift perturbations, induced by substrate analogue binding, suggest that the fully closed state is not adopted in the presence of lanthanide ions.
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Registered trials
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