[NMR paper] High-resolution crystal structures and STD NMR mapping of human ABO(H) blood group glycosyltransferases in complex with trisaccharide reaction products suggest a molecular basis for product release.
High-resolution crystal structures and STD NMR mapping of human ABO(H) blood group glycosyltransferases in complex with trisaccharide reaction products suggest a molecular basis for product release.
Related ArticlesHigh-resolution crystal structures and STD NMR mapping of human ABO(H) blood group glycosyltransferases in complex with trisaccharide reaction products suggest a molecular basis for product release.
Abstract
The human ABO(H) blood group A- and B-synthesizing glycosyltransferases GTA and GTB have been structurally characterized to high resolution in complex with their respective trisaccharide antigen products. These findings are particularly timely and relevant given the dearth of glycosyltransferase structures collected in complex with their saccharide reaction products. GTA and GTB utilize the same acceptor substrates, oligosaccharides terminating with ?-l-Fucp-(1->2)-?-d-Galp-OR (where R is a glycolipid or glycoprotein), but use distinct UDP donor sugars, UDP-N-acetylgalactosamine and UDP-galactose, to generate the blood group A (?-l-Fucp-(1->2)[?-d-GalNAcp-(1->3)]-?-d-Galp-OR) and blood group B (?-l-Fucp-(1->2)[?-d-Galp-(1->3)]-?-d-Galp-OR) determinant structures, respectively. Structures of GTA and GTB in complex with their respective trisaccharide products reveal a conflict between the transferred sugar monosaccharide and the ?-phosphate of the UDP donor. Mapping of the binding epitopes by saturation transfer difference NMR measurements yielded data consistent with the X-ray structural results. Taken together these data suggest a mechanism of product release where monosaccharide transfer to the H-antigen acceptor induces active site disorder and ejection of the UDP leaving group prior to trisaccharide egress.
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 methylâ??methyl NOESY
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 methylâ??methyl NOESY
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,...
Structural Basis for the Serratia marcescens Lipase Secretion System: Crystal Structures of the Membrane FusionProtein and Nucleotide-Binding Domain
Structural Basis for the Serratia marcescens Lipase Secretion System: Crystal Structures of the Membrane FusionProtein and Nucleotide-Binding Domain
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00985/20171109/images/medium/bi-2017-00985x_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00985
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11-11-2017 07:52 AM
[NMR paper] Epitope mapping of histo blood group antigens bound to norovirus VLPs using STD NMR experiments reveals fine details of molecular recognition.
Epitope mapping of histo blood group antigens bound to norovirus VLPs using STD NMR experiments reveals fine details of molecular recognition.
Epitope mapping of histo blood group antigens bound to norovirus VLPs using STD NMR experiments reveals fine details of molecular recognition.
Glycoconj J. 2017 Aug 19;:
Authors: Fiege B, Leuthold M, Parra F, Dalton KP, Meloncelli PJ, Lowary TL, Peters T
Abstract
Attachment of human noroviruses to histo blood group antigens (HBGAs) is thought to be critical for the infection process....
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08-22-2017 10:10 AM
Caught before Released: Structural Mapping of the Reaction Trajectory for the Sofosbuvir Activating Enzyme, Human Histidine Triad Nucleotide Binding Protein 1 (hHint1)
Caught before Released: Structural Mapping of the Reaction Trajectory for the Sofosbuvir Activating Enzyme, Human Histidine Triad Nucleotide Binding Protein 1 (hHint1)
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00148/20170710/images/medium/bi-2017-00148s_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00148
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07-11-2017 09:20 AM
[NMR paper] Protein NMR Studies of substrate binding to human blood group A and B glycosyltransferases.
Protein NMR Studies of substrate binding to human blood group A and B glycosyltransferases.
Related Articles Protein NMR Studies of substrate binding to human blood group A and B glycosyltransferases.
Chembiochem. 2017 Mar 03;:
Authors: Peters T, Grimm LL, Weissbach S, Flügge F, Begemann N, Palcic M
Abstract
Donor and acceptor substrate binding to human blood group A and B glycosyltransferases (GTA, GTB) has been studied by a variety of protein NMR experiments. Prior crystallographic studies have shown these enzymes to adopt an...
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03-04-2017 12:19 PM
[NMR paper] NMR Metabolomics Profiling of Blood Plasma Mimics shows that Medium- and Long-chain Fatty Acids Differently Release Metabolites from Human Serum Albumin
NMR Metabolomics Profiling of Blood Plasma Mimics shows that Medium- and Long-chain Fatty Acids Differently Release Metabolites from Human Serum Albumin
Publication date: Available online 12 December 2013
Source:Journal of Magnetic Resonance</br>
Author(s): M.D. Jupin , P.J. Michiels , F.C. Girard , M. Spraul , S.S. Wijmenga</br>
Metabolite profiling by NMR of body fluids is increasingly used to successfully differentiate patients from healthy individuals. Metabolites and their concentrations are direct reporters of body biochemistry. However, in blood plasma...
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12-12-2013 11:39 PM
Molecular dynamics re-refinement of two different small RNA loop structures using the original NMR data suggest a common structure
Molecular dynamics re-refinement of two different small RNA loop structures using the original NMR data suggest a common structure
Abstract Restrained molecular dynamics simulations are a robust, though perhaps underused, tool for the end-stage refinement of biomolecular structures. We demonstrate their utilityâ??using modern simulation protocols, optimized force fields, and inclusion of explicit solvent and mobile counterionsâ??by re-investigating the solution structures of two RNA hairpins that had previously been refined using conventional techniques. The structures, both domain 5...
High-resolution crystal structures and STD NMR mapping of human ABO(H) blood group glycosyltransferases in complex with trisaccharide reaction products suggest a molecular basis for product release.
Linear Mode
