Fold recognition study of alpha3-galactosyltransferase and molecular modeling of the nucleotide sugar-binding domain
| Autor: | Cédric Monier, Wolfgang Rüger, Paul S. Freemont, Manfred J. Sippl, Anne Imberty, Christelle Breton, Emmanuel Bettler, Solange Moréra, Hannes Flöckner |
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| Přispěvatelé: | Deleage, Gilbert, Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular Protein Folding Swine Stereochemistry Molecular Sequence Data macromolecular substances Biology Ligands Thioredoxin fold Biochemistry Protein Structure Secondary Uridine Diphosphate Galactose 03 medical and health sciences Glycogen phosphorylase Catalytic Domain [SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology Animals Humans [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence Protein secondary structure 030304 developmental biology Galactosyltransferase 0303 health sciences Sequence Homology Amino Acid 030302 biochemistry & molecular biology Galactosyltransferases Ligand (biochemistry) Globin fold Cyclic nucleotide-binding domain Binding domain |
| Zdroj: | Glycobiology Glycobiology, Oxford University Press (OUP), 1999, 9, pp.713-722 HAL |
| ISSN: | 1460-2423 0959-6658 |
| DOI: | 10.1093/glycob/9.7.713 |
| Popis: | International audience; The structure and fold of the enzyme responsible for the biosynthesis of the xenotransplantation antigen, namely pig alpha3 galactosyltransferase, has been studied by means of computational methods. Secondary structure predictions indicated that alpha3-galactosyltransferase and related protein family members, including blood group A and B transferases and Forssman synthase, are likely to consist of alternating alpha-helices and beta-strands. Fold recognition studies predicted that alpha3-galactosyltransferase shares the same fold as the T4 phage DNA-modifying enzyme beta-glucosyltransferase. This latter enzyme displays a strong structural resemblance with the core of glycogen phosphorylase b. By using the three-dimensional structure of beta-glucosyltransferase and of several glycogen phosphorylases, the nucleotide binding domain of pig alpha3-galactosyltransferase was built by knowledge-based methods. Both the UDP-galactose ligand and a divalent cation were included in the model during the refinement procedure. The final three-dimensional model is in agreement with our present knowledge of the biochemistry and mechanism of alpha3-galactosyltransferases.The structure and fold of the enzyme responsible for the biosynthesis of the xenotransplantation antigen, namely pig alpha3 galactosyltransferase, has been studied by means of computational methods. Secondary structure predictions indicated that alpha3-galactosyltransferase and related protein family members, including blood group A and B transferases and Forssman synthase, are likely to consist of alternating alpha-helices and beta-strands. Fold recognition studies predicted that alpha3-galactosyltransferase shares the same fold as the T4 phage DNA-modifying enzyme beta-glucosyltransferase. This latter enzyme displays a strong structural resemblance with the core of glycogen phosphorylase b. By using the three-dimensional structure of beta-glucosyltransferase and of several glycogen phosphorylases, the nucleotide binding domain of pig alpha3-galactosyltransferase was built by knowledge-based methods. Both the UDP-galactose ligand and a divalent cation were included in the model during the refinement procedure. The final three-dimensional model is in agreement with our present knowledge of the biochemistry and mechanism of alpha3-galactosyltransferases. |
| Databáze: | OpenAIRE |
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