Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate

Biochemical and Biophysical Research Communications

Volumn 383, Issue 1, 2009, Pages 83-87

  Teramoto, Takamasa ^a   Sakakibara, Yoichi ^b   Liu, Ming Cheh ^c   Suiko, Masahito ^b   Kimura, Makoto ^a   Kakuta, Yoshimitsu ^a  

^a KYUSHU UNIVERSITY   (Japan)

^b UNIVERSITY OF MIYAZAKI   (Japan)

^c MEDICAL COLLEGE OF OHIO   (United States)

Author keywords

Crystal structure; Michaelis complex; Sulfotransferase; Sulfuryl transfer reaction

Indexed keywords

ADENOSINE 3' PHOSPHATE 5' PHOSPHOSULFATE; HISTIDINE; LYSINE; NITROPHENOL; SULFOTRANSFERASE; SULFOTRANSFERASE 1D1; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL REACTION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE; MICHAELIS CONSTANT; MOLECULAR MECHANICS; MOUSE; NONHUMAN; PRIORITY JOURNAL; SULFONATION;

ANIMALS; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; HISTIDINE; LYSINE; MICE; NITROPHENOLS; PHOSPHOADENOSINE PHOSPHOSULFATE; PROTEIN CONFORMATION; SULFOTRANSFERASES;

EID: 67349237767     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.03.146     Document Type: Article

References (25)

1. Blanchard R.L., Freimuth R.R., Buck J., Weinshilboum R.M., and Coughtrie M.W. A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily. Pharmacogenetics 14 (2004) 199-211
2. Zhang H., Varlamova O., Vargas F.M., Falany C.N., and Leyh T.S. Sulfuryl transfer: the catalytic mechanism of human estrogen sulfotransferase. J. Biol. Chem. 273 (1998) 10888-10892
3. Falany C.N. Enzymology of human cytosolic sulfotransferases. FASEB J. 11 (1997) 206-216
4. Coughtrie M.W., Sharp S., Maxwell K., and Innes N.P. Biology, function of the reversible sulfation pathway catalysed by human sulfotransferases, sulfatases. Chem. Biol. Interact. 109 (1998) 3-27
5. Wang Y., Spitz M.R., Tsou A.M., Zhang K., Makan N., and Wu X. Sulfotransferase (SULT) 1A1 polymorphism as a predisposition factor for lung cancer: a case-control analysis. Lung Cancer 35 (2002) 137-142
6. Bamber D.E., Fryer A.A., Strange R.C., Elder J.B., Deakin M., Rajagopal R., Fawole A., Gilissen R.A., Campbell F.C., and Coughtrie M.W. Phenol sulphotransferase SULT1A1*1 genotype is associated with reduced risk of colorectal cancer. Pharmacogenetics 11 (2001) 679-685
7. Shimada M., Terazawa R., Kamiyama Y., Honma W., Nagata K., and Yamazoe Y. Unique properties of a renal sulfotransferase, St1d1, in dopamine metabolism. J. Pharmacol. Exp. Ther. 310 (2004) 808-814
8. Sakakibara Y., Yanagisawa K., Takami Y., Nakayama T., Suiko M., and Liu M.C. Molecular cloning expression and functional characterization of novel mouse sulfotransferases. Biochem. Biophys. Res. Commun. 247 (1998) 681-686
9. Teramoto T., Sakakibara Y., Inada K., Kurogi K., Liu M.C., Suiko M., Kimura M., and Kakuta Y. Crystal structure of MSULT1D1, a mouse catecholamine sulfotransferase. FEBS Lett. 582 (2008) 3909-3914
10. Teramoto T., Sakakibara Y., Liu M.C., Suiko M., Kimura M., and Kakuta Y. Structural basis for the broad range substrate specificity of a novel mouse cytosolic sulfotransferase-mSULT1D1. Biochem. Biophys. Res. Commun. 379 (2009) 76-80
11. Allali-Hassani A., Pan P.W., Dombrovski L., Najmanovich R., Tempel W., Dong A., Loppnau P., Martin F., Thornton J., Edwards A.M., Bochkarev A., Plotnikov A.N., Vedadi M., and Arrowsmith C.H. Structural and chemical profiling of the human cytosolic sulfotransferases. PLoS Biol. 5 (2007) e97
12. Negishi M., Pedersen L.G., Petrotchenko E., Shevtsov S., Gorokhov A., Kakuta Y., and Pedersen L.C. Structure and function of sulfotransferases. Arch. Biochem. Biophys. 390 (2001) 149-157
13. Chapman E., Best M.D., Hanson S.R., and Wong C.H. Sulfotransferases: structure, mechanism, biological activity, inhibition, and synthetic utility. Angew. Chem. Int. Ed. Engl. 43 (2004) 3526-3548
14. Kakuta Y., Pedersen L.G., Carter C.W., Negishi M., and Pedersen L.C. Crystal structure of estrogen sulphotransferase. Nat. Struct. Biol. 4 (1997) 904-908
15. Kakuta Y., Petrotchenko E.V., Pedersen L.C., and Negishi M. The sulfuryl transfer mechanism. Crystal structure of a vanadate complex of estrogen sulfotransferase and mutational analysis. J. Biol. Chem. 273 (1998) 27325-27330
16. Pedersen L.C., Petrotchenko E., Shevtsov S., and Negishi M. Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction. J. Biol. Chem. 277 (2002) 17928-17932
17. Hoff R.H., Czyryca P.G., Sun M., Leyh T.S., and Hengge A.C. Transition state of the sulfuryl transfer reaction of estrogen sulfotransferase. J. Biol. Chem. 281 (2006) 30645-30649
18. Lin P., Yang W., Pedersen L.C., Negishi M., and Pedersen L.G. Searching for the minimum energy path in the sulfuryl transfer reaction catalyzed by human estrogen sulfotransferase: role of enzyme dynamics. Int. J. Quantum Chem. 106 (2006) 2981-2998
19. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
20. Vagin A., and Teplyakov A. An approach to multi-copy search in molecular replacement. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 1622-1624
21. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53 (1997) 240-255
22. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 2126-2132
23. Vaguine A.A., Richelle J., and Wodak S.J. SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 191-205
24. Leyh T.S. The physical biochemistry and molecular genetics of sulfate activation. Crit. Rev. Biochem. Mol. Biol. 28 (1993) 515-542
25. Tyapochkin E., Cook P.F., and Chen G. Isotope exchange at equilibrium indicates a steady state ordered kinetic mechanism for human sulfotransferase. Biochemistry 47 (2008) 11894-11899