Crystal structure of α-1,3-galactosyltransferase (α3GT) in a complex with p-nitrophenyl-β-galactoside (pNPβGal)

Biochemical and Biophysical Research Communications

Volumn 385, Issue 4, 2009, Pages 601-604

  Jamaluddin, Haryati ^a   Tumbale, Percy ^b   Ferns, Tyrone A ^b   Thiyagarajan, Nethaji ^a   Brew, Keith ^b   Acharya, K Ravi ^a  

^a University of Bath   (United Kingdom)

^b FLORIDA ATLANTIC UNIVERSITY   (United States)

Author keywords

1,3 Galactosyltransferase; Crystal structure; Enzyme kinetics; Glycosyltransferase; Substrate binding

Indexed keywords

4 NITROPHENYL BETA GALACTOSIDE; ALPHA 1,3 GALACTOSYLTRANSFERASE; CARBOHYDRATE DERIVATIVE; N ACETYLGLUCOSAMINE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE;

ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; PRIORITY JOURNAL; WILD TYPE;

CRYSTALLOGRAPHY, X-RAY; GALACTOSYLTRANSFERASES; NITROPHENYLGALACTOSIDES; PROTEIN CONFORMATION;

EID: 67349094530     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.05.111     Document Type: Article

References (25)

1. Rudd P.M., Elliott T., Cresswell P., Wilson I.A., and Dwek R.A. Glycosylation and the immune system. Science 291 (2001) 2370-2376
2. Weijers C.A., Franssen M.C., and Visser G.M. Glycosyltransferase-catalyzed synthesis of bioactive oligosaccharides. Biotechnol. Adv. 26 (2008) 436-456
3. Persson M., and Palcic M.M. A high-throughput pH indicator assay for screening glycosyltransferase saturation mutagenesis libraries. Anal. Biochem. 378 (2008) 1-7
4. Aharoni A., Thiene K., Chiu C.P., Buchini S., Liarson L.L., Chen H., Strynadka N.C., Wakarchuk W.W., and Withers S.G. High-throughput screening methodology for the directed evolution of glycosyltransferases. Nat. Methods 3 (2006) 609-614
5. Lairson L.L., Watts A.G., Wakarchuk W.W., and Withers S.G. Using substrate engineering to harness enzymatic promiscuity and expand biological catalysis. Nat. Chem. Biol. 2 (2006) 724-728
6. Campbell J.A., Davies G.J., Bulone V., and Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 326 (1997) 929-939
7. Coutinho P.M., Deleury E., Davies G.J., and Henrissat B. An evolving hierarchical family classification for glycosyltransferases. J. Mol. Biol. 328 (2003) 307-317
8. Zhang Y., Wang P.G., and Brew K. Specificity and mechanism of metal ion activation in UDP-galactose β-galactoside α-1,3-galactosyltransferase. J. Biol. Chem. 276 (2001) 11567-11574
9. Tumbale P., Jamaluddin H., Thiyagarajan N., Acharya K.R., and Brew K. Screening a limited structure-based library identifies UDP-GalNAc-specific mutants of α-1,3 galactosyltransferase. Glycobiology 18 (2008) 1036-1043
10. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
11. Boix E., Swaminathan G.J., Zhang Y., Natesh R., Brew K., and Acharya K.R. Structure of UDP complex of UDP-galactose: β-galactoside-α-1,3-galactosyltransferase at 1.53 Å resolution reveals a conformational change in the catalytically important C-terminus. J. Biol. Chem. 276 (2001) 48608-48614
12. Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography, Acta Cryst. D 50 (1994) 760-763.
13. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Cryst. D 60 (2004) 2126-2132
14. Davis I.W., Leaver-Fay A., Chen V.B., Block J.N., Kapral G.J., Wang X., Murray L.W., Arendall W.B., Snoeyink J., Richardson J.S., and Richardson D.C. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35 (2007) W375-W383
15. Boix E., Swaminathan G.J., Zhang Y., Natesh R., Brew K., and Acharya K.R. Structural basis of ordered binding of donor and acceptor substrates to the retaining glycosyltransferase: α-1,3 galactosyltransferase. J. Biol. Chem. 277 (2002) 28310-28318
16. McDonald I.K., and Thornton J.M. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238 (1994) 777-793
17. Varki A. Nothing in glycobiology makes sense, except in the light of evolution. Cell 126 (2006) 841-845
18. Mackiewicz A., Dewey M.J., Berger F.G., and Baumann H. Acute phase mediated change in glycosylation of rat alpha 1-acid glycoprotein in transgenic mice. Glycobiology 1 (1991) 265-269
19. Dwek R.A. Glycobiology: toward understanding the function of sugars. Chem. Rev. 96 (1996) 683-720
20. Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3 (1993) 97-130
21. Springer T.A. Adhesion receptors of the immune system. Nature 346 (1990) 425-434
22. Galili U., Shohet S.B., Kobrin E., Stults C.L., and Macher B.A. Man, apes, and Old World monkeys differ from other mammals in the expression of α-galactosyl epitopes on nucleated cells. J. Biol. Chem. 263 (1988) 17755-17762
23. Galili U., and Swanson K. Gene sequences suggest inactivation of α-1,3-galactosyltransferase in catarrhines after the divergence of apes from monkeys. Proc. Natl. Acad. Sci. USA 88 (1991) 7401-7404
24. Carter P., and Wells J.A. Engineering enzyme specificity by substrate-assisted catalysis. Science 237 (1987) 394-399
25. Zhang Y., Deshpande A., Xie Z., Natesh R., Acharya K.R., and Brew K. Roles of active site tryptophans in substrate binding and catalysis by α-1,3 galactosyltransferase. Glycobiology 14 (2004) 1295-1302