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Volumn 75, Issue 2, 2009, Pages 289-295

An unusually small dimer interface is observed in all available crystal structures of cytosolic sulfotransferases

Author keywords

Biological interactions; Sulfotransferase; X ray crystallography

Indexed keywords

CYTOSOLIC SULFOTRANSFERASE; DIMER; SULFOTRANSFERASE; UNCLASSIFIED DRUG; ARABIDOPSIS PROTEIN;

EID: 66149131846     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22347     Document Type: Article
Times cited : (17)

References (34)
  • 4
    • 0025230526 scopus 로고
    • Purification and characterization of human liver phenol-sulfating phenol sulfotrans-ferase
    • Falany CN, Vazquez ME, Heroux JA, Roth JA. Purification and characterization of human liver phenol-sulfating phenol sulfotrans-ferase. Arch Biochem Biophys 1990;278:312-318.
    • (1990) Arch Biochem Biophys , vol.278 , pp. 312-318
    • Falany, C.N.1    Vazquez, M.E.2    Heroux, J.A.3    Roth, J.A.4
  • 5
    • 0026327647 scopus 로고
    • Purification of a rat liver phenol sulfotransferase (P-STG) with the aid of guanidine hydro-chloride treatment
    • Homma H, Kamakura M, Nakagome I, Matsui M. Purification of a rat liver phenol sulfotransferase (P-STG) with the aid of guanidine hydro-chloride treatment. Chem Pharm Bull (Tokyo) 1991;39:3307-3312.
    • (1991) Chem Pharm Bull (Tokyo) , vol.39 , pp. 3307-3312
    • Homma, H.1    Kamakura, M.2    Nakagome, I.3    Matsui, M.4
  • 6
    • 0028848909 scopus 로고
    • Homodimeric and heterodi-meric aryl sulfotransferases catalyze the sulfuric acid esterification of N-hydroxy-2-acetylaminofluorene
    • Kiehlbauch CC, Lam YF, Ringer DP. Homodimeric and heterodi-meric aryl sulfotransferases catalyze the sulfuric acid esterification of N-hydroxy-2-acetylaminofluorene. J Biol Chem 1995;270:18941-18947.
    • (1995) J Biol Chem , vol.270 , pp. 18941-18947
    • Kiehlbauch, C.C.1    Lam, Y.F.2    Ringer, D.P.3
  • 7
    • 0033152067 scopus 로고    scopus 로고
    • Kinetic properties of human dopamine sulfotrans-ferase (SULT1A3) expressed in prokaryotic and eukaryotic systems: Comparison with the recombinant enzyme purified from Escherichia coli
    • Dajani R, Sharp S, Graham S, Bethell SS, Cooke RM, Jamieson DJ, Coughtrie MW. Kinetic properties of human dopamine sulfotrans-ferase (SULT1A3) expressed in prokaryotic and eukaryotic systems: comparison with the recombinant enzyme purified from Escherichia coli. Protein Expr Purif 1999;16:11-18.
    • (1999) Protein Expr Purif , vol.16 , pp. 11-18
    • Dajani, R.1    Sharp, S.2    Graham, S.3    Bethell, S.S.4    Cooke, R.M.5    Jamieson, D.J.6    Coughtrie, M.W.7
  • 9
    • 0025323099 scopus 로고
    • Purification and some characteristics of an oestrogen sulfotransferase from guinea pig adrenal gland and its non-identity with adrenal pregnenolone sulfotransfer-ase
    • Hobkirk R, Glasier MA, Brown LY. Purification and some characteristics of an oestrogen sulfotransferase from guinea pig adrenal gland and its non-identity with adrenal pregnenolone sulfotransfer-ase. Biochem J 1990;268:759-764.
    • (1990) Biochem J , vol.268 , pp. 759-764
    • Hobkirk, R.1    Glasier, M.A.2    Brown, L.Y.3
  • 10
    • 0021814378 scopus 로고
    • The purification of 3 beta-hydroxysteroid sulfotransferase of the hamster epidi-dymis
    • Bouthillier M, Bleau G, Chapdelaine A, Roberts KD. The purification of 3 beta-hydroxysteroid sulfotransferase of the hamster epidi-dymis. J Steroid Biochem 1985;22:733-738.
    • (1985) J Steroid Biochem , vol.22 , pp. 733-738
    • Bouthillier, M.1    Bleau, G.2    Chapdelaine, A.3    Roberts, K.D.4
  • 11
    • 0024401919 scopus 로고
    • Purification and characterization of human liver dehydroepiandrosterone sulfotransferase
    • Falany CN, Vazquez ME, Kalb JM. Purification and characterization of human liver dehydroepiandrosterone sulfotransferase. Biochem J 1989;260:641-646.
    • (1989) Biochem J , vol.260 , pp. 641-646
    • Falany, C.N.1    Vazquez, M.E.2    Kalb, J.M.3
  • 12
    • 0028206388 scopus 로고
    • Major hydroxysteroid sulfotransferase STa in rat liver cytosol may consist of two microheterogeneous subunits
    • Ogura K, Satsukawa M, Okuda H, Hiratsuka A, Watabe T. Major hydroxysteroid sulfotransferase STa in rat liver cytosol may consist of two microheterogeneous subunits. Chem Biol Interact 1994;92 (1-3):129-144.
    • (1994) Chem Biol Interact , vol.92 , Issue.1-3 , pp. 129-144
    • Ogura, K.1    Satsukawa, M.2    Okuda, H.3    Hiratsuka, A.4    Watabe, T.5
  • 13
    • 0034625464 scopus 로고    scopus 로고
    • Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase
    • Pedersen LC, Petrotchenko EV, Negishi M. Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase. FEBS Lett 2000; 475:61-64.
    • (2000) FEBS Lett , vol.475 , pp. 61-64
    • Pedersen, L.C.1    Petrotchenko, E.V.2    Negishi, M.3
  • 14
    • 33646379631 scopus 로고    scopus 로고
    • A novel sulfo-transferase abundantly expressed in the dauer larvae of Caenorhab-ditis elegans
    • Hattori K, Inoue M, Inoue T, Arai H, Tamura HO. A novel sulfo-transferase abundantly expressed in the dauer larvae of Caenorhab-ditis elegans. J Biochem 2006;139:355-362.
    • (2006) J Biochem , vol.139 , pp. 355-362
    • Hattori, K.1    Inoue, M.2    Inoue, T.3    Arai, H.4    Tamura, H.O.5
  • 17
    • 20844462588 scopus 로고    scopus 로고
    • MollDE: A homology modeling framework you can click with
    • Canutescu AA, Dunbrack RL, Jr. MollDE: a homology modeling framework you can click with. Bioinformatics 2005;21:2914-2916.
    • (2005) Bioinformatics , vol.21 , pp. 2914-2916
    • Canutescu, A.A.1    Dunbrack Jr, R.L.2
  • 18
    • 56349095598 scopus 로고    scopus 로고
    • SCWRL and MolIDE: Programs for protein side-chain prediction and homology modeling
    • Wang Q, Canutescu AA, Dunbrack RL, Jr. SCWRL and MolIDE: programs for protein side-chain prediction and homology modeling. Nat Protoc 2008;3:1832-1847.
    • (2008) Nat Protoc , vol.3 , pp. 1832-1847
    • Wang, Q.1    Canutescu, A.A.2    Dunbrack Jr, R.L.3
  • 21
    • 66449108663 scopus 로고    scopus 로고
    • Hubbard SJ, Thornton JM. NACCESS. London: Department of Biochemistry and Molecular Biology, University College London; 1993.
    • Hubbard SJ, Thornton JM. NACCESS. London: Department of Biochemistry and Molecular Biology, University College London; 1993.
  • 22
    • 33751357065 scopus 로고    scopus 로고
    • ProtBuD: A database of biological unit structures of protein families and super-families
    • Xu Q, Canutescu A, Obradovic Z, Dunbrack RL, Jr. ProtBuD: a database of biological unit structures of protein families and super-families. Bioinformatics 2006;22:2876-2882.
    • (2006) Bioinformatics , vol.22 , pp. 2876-2882
    • Xu, Q.1    Canutescu, A.2    Obradovic, Z.3    Dunbrack Jr, R.L.4
  • 24
    • 0032169688 scopus 로고    scopus 로고
    • PQS: A protein quaternary structure file server
    • Henrick K, Thornton JM. PQS: a protein quaternary structure file server. Trends Biochem Sci 1998;23:358-361.
    • (1998) Trends Biochem Sci , vol.23 , pp. 358-361
    • Henrick, K.1    Thornton, J.M.2
  • 25
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K. Inference of macromolecular assemblies from crystalline state. J Mol Biol 2007;372:774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 26
    • 16344364140 scopus 로고    scopus 로고
    • PDBML: The representation of archival macromolecular structure data in XML
    • Westbrook J, Ito N, Nakamura H, Henrick K, Berman HM. PDBML: the representation of archival macromolecular structure data in XML. Bioinformatics 2005;21:988-992.
    • (2005) Bioinformatics , vol.21 , pp. 988-992
    • Westbrook, J.1    Ito, N.2    Nakamura, H.3    Henrick, K.4    Berman, H.M.5
  • 27
    • 1642453680 scopus 로고    scopus 로고
    • Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfo-transferase (DHEA-ST) important for steroid homeostasis: Structure of the enzyme-ADT complex
    • Chang HJ, Shi R, Rehse P, Lin SX. Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfo-transferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex. J Biol Chem 2004;279:2689-2696.
    • (2004) J Biol Chem , vol.279 , pp. 2689-2696
    • Chang, H.J.1    Shi, R.2    Rehse, P.3    Lin, S.X.4
  • 28
    • 0042386609 scopus 로고    scopus 로고
    • The relationship between sequence and interaction divergence in proteins
    • Aloy P, Ceulemans H, Stark A, Russell RB. The relationship between sequence and interaction divergence in proteins. J Mol Biol 2003;332:989-998.
    • (2003) J Mol Biol , vol.332 , pp. 989-998
    • Aloy, P.1    Ceulemans, H.2    Stark, A.3    Russell, R.B.4
  • 29
    • 0037745545 scopus 로고    scopus 로고
    • Crystallo-graphic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase
    • Shevtsov S, Petrotchenko EV, Pedersen LC, Negishi M. Crystallo-graphic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase. Environ Health Perspect 2003;111:884-888.
    • (2003) Environ Health Perspect , vol.111 , pp. 884-888
    • Shevtsov, S.1    Petrotchenko, E.V.2    Pedersen, L.C.3    Negishi, M.4
  • 33
    • 33645287012 scopus 로고    scopus 로고
    • Gene-environment interaction: The role of SULT1A1 and CYP3A5 polymorphisms as risk modifiers for squamous cell carcinoma of the esophagus
    • Dandara C, Li DP, Walther G, Parker MI. Gene-environment interaction: the role of SULT1A1 and CYP3A5 polymorphisms as risk modifiers for squamous cell carcinoma of the esophagus. Carcino-genesis 2006;27:791-797.
    • (2006) Carcino-genesis , vol.27 , pp. 791-797
    • Dandara, C.1    Li, D.P.2    Walther, G.3    Parker, M.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.