Base-modified donor analogues reveal novel dynamic features of a glycosyltransferase

Journal of Biological Chemistry

Volumn 288, Issue 36, 2013, Pages 26201-26208

  Jørgensen, René ^a,b   Pesnot, Thomas ^c   Lee, Ho Jun ^d   Palcic, Monica M ^b   Wagner, Gerd K ^e  

^a STATENS SERUM INSTITUT   (Denmark)

^b CARLSBERG LABORATORY   (Denmark)

^c UNIVERSITY OF EAST ANGLIA   (United Kingdom)

^d UNIVERSITY OF ALBERTA   (Canada)

^e KING'S COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL CHANGE; CONFORMATIONAL PLASTICITY; DONOR SUBSTRATES; DYNAMIC FEATURES; GLYCOSYL TRANSFERASE; GLYCOSYLTRANSFERASES; STRUCTURAL STUDIES;

BIOCHEMISTRY; BIOLOGY;

ENZYME INHIBITION;

5 FORMYLTHIENYL DERIVATIVE; GLYCOSYLTRANSFERASE; UNCLASSIFIED DRUG; URACIL DERIVATIVE; URIDINE DIPHOSPHATE GALACTOSE;

ARTICLE; BLOOD GROUP; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CHEMICAL MODIFICATION; CONTROLLED STUDY; DRUG TARGETING; ENZYME BINDING; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME KINETICS; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FOLDING;

CRYSTALLOGRAPHY; ENZYME INHIBITORS; GLYCOSYLTRANSFERASES; KINETICS; MOLECULAR DYNAMICS;

ABO BLOOD-GROUP SYSTEM; AMINO ACID MOTIFS; CATALYSIS; ENZYME INHIBITORS; HUMANS; N-ACETYLGALACTOSAMINYLTRANSFERASES; URIDINE DIPHOSPHATE GALACTOSE; URIDINE DIPHOSPHATE N-ACETYLGALACTOSAMINE;

EID: 84883705379     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.465963     Document Type: Article

References (28)

1. Lairson, L. L., Henrissat, B., Davies, G. J., and Withers, S. G. (2008) Glycosyltransferases: structures, functions, and mechanisms. Annu. Rev. Biochem. 77, 521-555
2. Weadge, J. T., and Palcic, M. M. (2008) Wiley Encyclopedia of Chemical Biology (Begley, T. P., ed) Vol. 2, pp. 198-211, John Wiley & Sons, New York
3. Yamamoto, F., Cid, E., Yamamoto, M., and Blancher, A. (2012) ABO research in the modern era of genomics. Transfus. Med. Rev. 26, 103-118
4. Yamamoto, M., Lin, X. H., Kominato, Y., Hata, Y., Noda, R., Saitou, N., and Yamamoto, F. (2001) Murine equivalent of the human histo-blood group ABO gene is a cis-AB gene and encodes a glycosyltransferase with both A and B transferase activity. J. Biol. Chem. 276, 13701-13708
5. Alfaro, J. A., Zheng, R. B., Persson, M., Letts, J. A., Polakowski, R., Bai, Y., Borisova, S. N., Seto, N. O., Lowary, T. L., Palcic, M. M., and Evans, S. V. (2008) ABO(H) blood group A and B glycosyltransferases recognize substrate via specific conformational changes. J. Biol. Chem. 283, 10097-10108
6. Kamath, V. P., Seto, N. O., Compston, C. A., Hindsgaul, O., and Palcic, M. M. (1999) Synthesis of the acceptor analogue Fuc(132) Gal- O(CH2)7 CH3: a probe for the kinetic mechanism of recombinant human blood group B glycosyltransferase. Glycoconj. J. 16, 599-606
7. Qasba, P. K., Ramakrishnan, B., and Boeggeman, E. (2005) Substrate-induced conformational changes in glycosyltransferases. Trends Biochem. Sci. 30, 53-62
8. Pesnot, T., Jørgensen, R., Palcic, M. M., and Wagner, G. K. (2010) Structural and mechanistic basis for a new mode of glycosyltransferase inhibition. Nat. Chem. Biol. 6, 321-323
9. Rillahan, C. D., Antonopoulos, A., Lefort, C. T., Sonon, R., Azadi, P., Ley, K., Dell, A., Haslam, S. M., and Paulson, J. C. (2012) Global metabolic inhibitors of sialyl- and fucosyltransferases remodel the glycome. Nat. Chem. Biol. 8, 661-668
10. Gloster, T. M., Zandberg, W. F., Heinonen, J. E., Shen, D. L., Deng, L., and Vocadlo, D. J. (2011) Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells. Nat. Chem. Biol. 7, 174-181
11. Breton, C., Fournel-Gigleux, S., and Palcic, M. M. (2012) Recent structures, evolution and mechanisms of glycosyltransferases. Curr. Opin. Struct. Biol. 22, 540-549
12. Descroix, K., Pesnot, T., Yoshimura, Y., Gehrke, S. S., Wakarchuk, W., Palcic, M. M., and Wagner, G. K. (2012) Inhibition of galactosyltransferases by a novel class of donor analogues. J. Med. Chem. 55, 2015-2024
13. . Seto, N. O., Palcic, M. M., Compston, C. A., Li, H., Bundle, D. R., and Narang, S. A. (1997) Sequential interchange of four amino acids from blood group B to blood group A glycosyltransferase boosts catalytic activity and progressively modifies substrate recognition in human recombinant enzymes. J. Biol. Chem. 272, 14133-14138
14. Seto, N. O., Palcic, M. M., Hindsgaul, O., Bundle, D. R., and Narang, S. A. (1995) Expression of a recombinant human glycosyltransferase from a synthetic gene and its utilization for synthesis of the human blood group B trisaccharide. Eur. J. Biochem. 234, 323-328
15. Yazer, M. H., Zheng, R. B., Seto, N. O., Rose, N. L., Cho, D., and Palcic, M. M. (2005) Kinetic studies on Korean serum cis-AB enzymes reveal diminished A and B transferase activities. Vox Sang 89, 161-167
16. Gegner, J. A., and Dahlquist, F. W. (1991) Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA. Proc. Natl. Acad. Sci. U.S.A. 88, 750-754
17. Seto, N. O., Compston, C. A., Szpacenko, A., and Palcic, M. M. (2000) Enzymatic synthesis of blood group A and B trisaccharide analogues. Carbohydr. Res. 324, 161-169
18. Laferté, S., Chan, N. W., Sujino, K., Lowary, T. L., and Palcic, M. M. (2000) Intracellular inhibition of blood group A glycosyltransferase. Eur. J. Biochem. 267, 4840-4849
19. Kabsch, W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800
20. McCoy, A. J., Grosse-Kunstleve, R. W., Storoni, L. C., and Read, R. J. (2005) Likelihood-enhanced fast translation functions. Acta Crystallogr. D Biol. Crystallogr. 61, 458-464
21. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53, 240-255
22. Emsley, P., and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132
23. Adams, P. D., Grosse-Kunstleve, R. W., Hung, L. W., Ioerger, T. R., Mc- Coy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., and Terwilliger, T. C. (2002) PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D Biol. Crystallogr. 58, 1948-1954
24. Painter, J., and Merritt, E. A. (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. D Biol. Crystallogr. 62, 439-450
25. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
26. Boix, E., Swaminathan, G. J., Zhang, Y., Natesh, R., Brew, K., and Acharya, K. R. (2001) Structure of UDP complex of UDP-galactose:-galactoside-1, 3-galactosyltransferase at 1.53 A resolution reveals a conformational change in the catalytically important C terminus. J. Biol. Chem. 276, 48608-48614
27. Jørgensen, R., Grimm, L. L., Sindhuwinata, N., Peters, T., and Palcic, M. M. (2012) A glycosyltransferase inhibitor from a molecular fragment library simultaneously interferes with metal ion and substrate binding. Angew. Chem. Int. Ed. Engl. 51, 4171-4175
28. Martin, M. P., Zhu, J. Y., Lawrence, H. R., Pireddu, R., Luo, Y., Alam, R., Ozcan, S., Sebti, S. M., Lawrence, N. J., and Schönbrunn, E. (2012) A novel mechanism by which small molecule inhibitors induce the DFG flip in Aurora A. ACS Chem. Biol. 7, 698-706