Crystal structures of SULT1A2 and SULT1A1*3: Insights into the substrate inhibition and the role of Tyr149 in SULT1A2

Biochemical and Biophysical Research Communications

Volumn 396, Issue 2, 2010, Pages 429-434

  Lu, Jinghua ^a   Li, Haitao ^a   Zhang, Jiping ^a   Li, Mei ^a   Liu, Ming Yih ^b   An, Xiaomin ^a   Liu, Ming Cheh ^c   Chang, Wenrui ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b NATIONAL SYNCHROTRON RADIATION RESEARCH CENTER   (Taiwan)

^c MEDICAL COLLEGE OF OHIO   (United States)

Author keywords

Crystal structure; Cytosolic sulfotransferase; SULT; SULT1A1*3; SULT1A2

Indexed keywords

4 NITROPHENOL; ADENOSINE 3',5' DIPHOSPHATE; HISTIDINE; PHENYLALANINE; RIBONUCLEOTIDE; SULFOTRANSFERASE; SULFOTRANSFERASE 1A2; SULFOTRANSFERASE 1A3; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ASSAY; HUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SITE DIRECTED MUTAGENESIS; SULFONATION; WILD TYPE;

ARYLSULFOTRANSFERASE; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; HUMANS; MUTAGENESIS, SITE-DIRECTED; MUTATION; NITROPHENOLS; PHOSPHOADENOSINE PHOSPHOSULFATE; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; TYROSINE;

VERTEBRATA;

EID: 77952745911     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.04.109     Document Type: Article

References (44)

1. Strott C.A. Steroid sulfotransferases. Endocr. Rev. 17 (1996) 670-697
2. Falany C.N. Enzymology of human cytosolic sulfotransferases. FASEB J. 11 (1997) 206-216
3. Coughtrie M.W., Sharp S., Maxwell K., and Innes N.P. Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sulfatases. Chem. Biol. Interact. 109 (1998) 3-27
4. Glatt H. Sulfation and sulfotransferases 4: bioactivation of mutagens via sulfation. FASEB J. 11 (1997) 314-321
5. Glatt H. Sulfotransferases in the bioactivation of xenobiotics. Chem. Biol. Interact. 129 (2000) 141-170
6. Glatt H., Engelke C.E., Pabel U., Teubner W., Jones A.L., Coughtrie M.W., Andrae U., Falany C.N., and Meinl W. Sulfotransferases: genetics and role in toxicology. Toxicol. Lett. 112-113 (2000) 341-348
7. Falany C.N., Xie X., Wang J., Ferrer J., and Falany J.L. Molecular cloning and expression of novel sulphotransferase-like cDNAs from human and rat brain. Biochem. J. 346 Pt. 3 (2000) 857-864
8. Brix L.A., Barnett A.C., Duggleby R.G., Leggett B., and McManus M.E. Analysis of the substrate specificity of human sulfotransferases SULT1A1 and SULT1A3: site-directed mutagenesis and kinetic studies. Biochemistry 38 (1999) 10474-10479
9. Dajani R., Cleasby A., Neu M., Wonacott A.J., Jhoti H., Hood A.M., Modi S., Hersey A., Taskinen J., Cooke R.M., Manchee G.R., and Coughtrie M.W. X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity. J. Biol. Chem. 274 (1999) 37862-37868
10. Adjei A.A., and Weinshilboum R.M. Catecholestrogen sulfation: possible role in carcinogenesis. Biochem. Biophys. Res. Commun. 292 (2002) 402-408
11. Meinl W., Meerman J.H., and Glatt H. Differential activation of promutagens by alloenzymes of human sulfotransferase 1A2 expressed in Salmonella typhimurium. Pharmacogenetics 12 (2002) 677-689
12. Li X., Clemens D.L., Cole J.R., and Anderson R.J. Characterization of human liver thermostable phenol sulfotransferase (SULT1A1) allozymes with 3,3′,5-triiodothyronine as the substrate. J. Endocrinol. 171 (2001) 525-532
13. Stanley E.L., Hume R., Visser T.J., and Coughtrie M.W. Differential expression of sulfotransferase enzymes involved in thyroid hormone metabolism during human placental development. J. Clin. Endocrinol. Metab 86 (2001) 5944-5955
14. Raftogianis R.B., Wood T.C., Otterness D.M., Van Loon J.A., and Weinshilboum R.M. Phenol sulfotransferase pharmacogenetics in humans: association of common SULT1A1 alleles with TS PST phenotype. Biochem. Biophys. Res. Commun. 239 (1997) 298-304
15. Raftogianis R.B., Wood T.C., and Weinshilboum R.M. Human phenol sulfotransferases SULT1A2 and SULT1A1: genetic polymorphisms, allozyme properties, and human liver genotype-phenotype correlations. Biochem. Pharmacol. 58 (1999) 605-616
16. Glatt H.R. An overview of bioactivation of chemical carcinogens. Biochem. Soc. Trans. 28 (2000) 1-6
17. 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
18. Gamage N.U., Duggleby R.G., Barnett A.C., Tresillian M., Latham C.F., Liyou N.E., McManus M.E., and Martin J.L. Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition. J. Biol. Chem. 278 (2003) 7655-7662
19. 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
20. Bidwell L.M., McManus M.E., Gaedigk A., Kakuta Y., Negishi M., Pedersen L., and Martin J.L. Crystal structure of human catecholamine sulfotransferase. J. Mol. Biol. 293 (1999) 521-530
21. Lu J.H., Li H.T., Liu M.C., Zhang J.P., Li M., An X.M., and Chang W.R. Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3′-phosphoadenosine 5′-phosphate. Biochem. Biophys. Res. Commun. 335 (2005) 417-423
22. Pedersen L.C., Petrotchenko E.V., and Negishi M. Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase. FEBS Lett. 475 (2000) 61-64
23. Lee K.A., Fuda H., Lee Y.C., Negishi M., Strott C.A., and Pedersen L.C. Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3′-phosphoadenosine 5′-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. J. Biol. Chem. 278 (2003) 44593-44599
24. Sakakibara Y., Takami Y., Nakayama T., Suiko M., and Liu M.C. Localization and functional analysis of the substrate specificity/catalytic domains of human M-form and P-form phenol sulfotransferases. J. Biol. Chem. 273 (1998) 6242-6247
25. Liu M.C., Suiko M., and Sakakibara Y. Mutational analysis of the substrate binding/catalytic domains of human M form and P form phenol sulfotransferases. J. Biol. Chem. 275 (2000) 13460-13464
26. Otwinowski Z.M.W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
27. Vagin A., and Teplyakov A. Molecular replacement with MOLREP. Acta Crystallogr. D Biol. Crystallogr. 66 (2010) 22-25
28. Navaza J. AMoRe: an automated package for molecular replacement. Acta Cryst. 50 (1994) 157-163
29. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., and Warren G.L. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54 (1998) 905-921
30. Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 Pt. 2 (1991) 110-119
31. Laskowski R.A. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26 (1993) 283-291
32. Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24 (1991) 946-950
33. Merritt E.A., and Murphy M.E. Raster3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 869-873
34. W.L. Delano, The PyMOL Molecular Graphics System, 2002. Available from: .
35. Barnett A.C., Tsvetanov S., Gamage N., Martin J.L., Duggleby R.G., and McManus M.E. Active site mutations and substrate inhibition in human sulfotransferase 1A1 and 1A3. J. Biol. Chem. 279 (2004) 18799-18805
36. Rossi A.M., Maggini V., Fredianelli E., Di B.D., Pietrabissa A., Mosca F., Barale R., and Pacifici G.M. Phenotype-genotype relationships of SULT1A1 in human liver and variations in the IC50 of the SULT1A1 inhibitor quercetin. Int. J. Clin. Pharmacol. Ther. 42 (2004) 561-567
37. Zhu X., Veronese M.E., Iocco P., and McManus M.E. CDNA Cloning and expression of a new form of human aryl sulfotransferase. Int. J. Biochem. Cell Biol. 28 (1996) 565-571
38. Fail-Isom L., Shui X., and Williams L.D. Divalent cations stabilize unstacked conformations of DNA and RNA by interacting with base pi systems. Biochemistry 37 (1998) 17105-17111
39. Mishiro E., Liu M.Y., Sakakibara Y., Suiko M., and Liu M.C. Zebrafish tyrosylprotein sulfotransferase: molecular cloning, expression, and functional characterization. Biochem. Cell Biol. 82 (2004) 295-303
40. Xu F., Suiko M., Sakakibara Y., Pai T.G., and Liu M.C. Regulatory effects of divalent metal cations on human cytosolic sulfotransferases. J. Biochem. 132 (2002) 457-462
41. Kooystra P.J., Kalk K.H., and Hol W.G. Soaking in Cs2SO4 reveals a caesium-aromatic interaction in bovine-liver rhodanese. Eur. J. Biochem. 177 (1988) 345-349
42. Liaw S.H., Kuo I., and Eisenberg D. Discovery of the ammonium substrate site on glutamine synthetase, a third cation binding site. Protein Sci. 4 (1995) 2358-2365
43. Labesse G., Ferrari D., Chen Z.W., Rossi G.L., Kuusk V., McIntire W.S., and Mathews F.S. Crystallographic and spectroscopic studies of native, aminoquinol, and monovalent cation-bound forms of methylamine dehydrogenase from Methylobacterium extorquens AM1. J. Biol. Chem. 273 (1998) 25703-25712
44. +-Trp) interactions in the crystal structure of tetragonal lysozyme. Protein Sci. 7 (1998) 2472-2475