A homology model for the human theta-class glutathione transferase T1-1

Proteins: Structure, Function and Genetics

Volumn 33, Issue 3, 1998, Pages 444-454

  Flanagan, J U ^a   Rossjohn, J ^b   Parker, M W ^b   Board, P G ^a   Chelvanayagam, G ^a  

^a Biology and Environment   (Australia)

^b ST VINCENT'S INSTITUTE OF MEDICAL RESEARCH   (Australia)

Author keywords

Dehalogenase; Dichloromethane; HGSTT1 1; Homology modeling; Menaphthyl sulfate

Indexed keywords

GLUTATHIONE TRANSFERASE;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CYCLIZATION; DATA BASE; DEHALOGENATION; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; GENE DELETION; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR MODEL; PRIORITY JOURNAL; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; DIMERIZATION; GLUTATHIONE TRANSFERASE; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

EID: 0032533759     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19981115)33:3<444::AID-PROT12>3.0.CO;2-8     Document Type: Article

References (45)

1. Mannervik, B., Danielson, U.H. Glutathione transferases: Structure and catalytic activity. CRC Crit. Rev. Biochem. 23:283-337, 1988.
2. Hayes, J.D., Pulford, D.J. The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. CRC Crit. Rev. Biochem. Mol. Biol., 30:445-600, 1995.
3. Meyer, D.J., Thomas, M. Characterization of rat spleen prostaglandin H D-isomerase as a sigma class GSH transferase. Biochem. J., 311:739-742, 1995.
4. Kanaoka, Y., Ago, H., Inagaki, E. et al. Cloning and crystal structure of hematopoietic prostaglandin D synthase. Cell 90:1085-1095, 1997.
5. Board, P.G., Baker, R.T., Chelvanayagam, G., Jermin, L.S. Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochem. J. 328:929-935, 1997.
6. Pemble, S.E, Wardle, A.F., Taylor, J.B. Glutathione S-transferase class Kappa: Characterization by the cloning of rat mitochondrial GST and identification of a human homologue. Biochem. J. 319:749-754, 1996.
7. Harris, J.M., Meyer, D.J., Coles, B., Ketterer, B. A novel glutathione transferase (13-13) isolated from the matrix of rat liver mitochondria having structural similarity to class Theta enzymes. Biochem. J., 278:137-141, 1991.
8. Chang, L-H., Chuang, L-F, Tsai, C-P, Tu, C-P.D., Tam, M.F. Characterization of glutathione s-transferases from day-old chick livers. Biochemistry 29:744-750, 1990.
9. Sinning, I., Kleywegt, G.J., Cowan, S.W. et al. Structure determination and refinement of human Alpha class glutathione transferase A1-1, and a comparison with Mu and Pi class enzymes. J. Mol. Biol. 232:192-212, 1993.
10. Ji, X., Zhang, P., Armstrong, R.N., Gilliland, G.L. The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2Å resolution. Biochemistry 31:10169-10184, 1992.
11. Reinemer, P., Dirr, H.W., Ladenstein, R., Schaffer, J., Gallay, O., Huber, R. The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution. EMBO J. 10:1997-2005, 1991.
12. Reinemer, P., Dirr, H.W., Ladenstein, R. et al. Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution. J. Mol. Biol. 227:214-226, 1992.
13. McTigue, M.A., Williams, D.R., Tainer, J.A. Crystal structures of a schitosomal drug and vaccine target: Glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistsomal drug praziquantel. J. Mol. Biol. 246:21-27, 1995.
14. Rossjohn, J., Feil, S.C., Wilce, M.C.J., Sexton, J.L., Spithill, T.W., Parker, M.W. Crystallization, structural determination and analysis of a novel parasite vaccine candidate: Fasciola hepatica glutathione S-transferase. J. Mol. Biol. 273:857-872, 1997.
15. Neuefeind, T., Huber, R., Reinemer, P. et al. Cloning, sequencing, crystallization, and X-ray structure of glutathione S-transferase-III from Zea mays var.mutin: A leading enzyme in detoxification of maize herbicides. J. Mol. Biol. 274:577-587, 1997.
16. Ji, X., von Rosenvinge, E.C., Johnson, W.W. et al. Three-dimensional structure, catalytic properties and evolution of Sigma class glutathione transferase from squid, a progenitor of the lense S-crystallins of cephalopods. Biochemistry. 34:5317-5328, 1995.
17. Wilce, M.C.J., Board, P.G., Feil, S.C., Parker, M.W. Crystal structure of a Theta-class glutathione transferase. EMBO J. 14:2133-2143, 1995
18. Reinemer, P., Prade, L., Hof, P. et al. Three-dimensional structure of glutathione s-transferase from Arabidopsis thaliana at 2.2Å resolution: Structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture. J. Mol. Biol., 255:289-309, 1996.
19. Dirr, H., Reinemer, P., and Huber, R. X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition, and catalytic function. Eur. J. Biochem. 220:645-661, 1994.
20. Rossjohn, J., McKinstry, W.J., Oakley, A.J. et al. The crystal structure of human Theta class glutathione transferase has a sulfate binding pocket within a buried active site. Structure 6:309-322 1998.
21. Chelvanayagam, G., Wilce, M.C.J., Parker, M.W., Tan, K.L., Board, P.G. Homology model for the human GSTT2 theta class glutathione transferase. Proteins 27:118-130, 1997.
22. Thomson, J.D., Higgins, D.G., Gibson, T.J. Clustal W: Improving the sensitivity of progressive multiple sequence alignments through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680, 1994.
23. Chelvanayagam, G., Eggenschwiller, A., Knecht, L., Gonnet, G., Benner S.A. An analysis of simultaneous variation in protein structures. Protein Eng. 10:307-316, 1997.
24. Rost, B., Sander, C. Prediction of protein structure at better than 70% accuracy. J. Mol. Biol. 232:584-599, 1993.
25. Rost, B. Sander, C., Schneider R. PHD-an automatic mail server for protein secondary structure prediction. CABIOS 10:53-60, 1994.
26. Rost, B., Sander, C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19:55-72, 1994.
27. Benner, S.A., Cannarozzi, G., Gerloff, D., Turcotte, M., Chelvanayagam G. Bona Fide predictions of protein secondary structure using transparent analyses of multiple sequence alignments. Chem. Rev. 97:2725-2843, 1997.
28. Lastowski, R.A., MacArthur, M.W., Moss, D.J., Thornton, J.M. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:283-291, 1993.
29. Jones, D., Taylor, W.R., Thornton, J. A new approach to fold recognition. Nature. 358:86-89, 1992.
30. Göbel, U., Sander, C., Scheider, R., Valencia, A. Correlated mutations and residue contacts in proteins. Proteins 18: 309-317, 1994.
31. Neher, E. How frequent are correlated changes in families of protein sequences? Proc. Natl. Acad. Sci. USA 91:98-102, 1994.
32. Shindyalov, I.N, Kolchanov, N.A., Sander, C. Can three-dimensional contacts in protein structures be predicted by analysis of correlated mutations. Protein Eng. 7:349-358, 1994.
33. Taylor, W.R., Hatrick, K. Compensating changes in protein multiple sequence alignments. Protein Eng. 7:341-348, 1994.
34. Meyer, D.J., Coles, B., Pemble, S.E., Gilmore, K.S., Fraser, G.M., Ketterer, B. Theta, a new class of glutathione transferases purified from rat and man. Biochem. J. 274: 409-414, 1991
35. Marsh, A., Fergusson, D.M. Knowledge based modelling of a bacterial dichloromethane dehalogenase. Proteins 28:217-226, 1997
36. Hsiao, C-D., Martsen, E.O., Lee, J-Y., Tsai, S-P, Tam, M.F. Amino acid sequencing, molecular cloning and modelling of the chick liver class-Theta glutathione S-transferase CL1. Biochem. J. 312:91-98, 1995.
37. Jemth, P., Mannervik, B. Kinetic characterization of recombinant human glutathione transferase T1-1, a polymorphic detoxication enzyme. Arch. Biochem. Biophys. 348:247-254, 1997.
38. Board, P.G., Coggan, M., Wilce, M.C.J., Parker, M.W. Evidence for an essential serine in the active site of the Theta class glutathione transferases. Biochem. J. 311:247-250, 1995.
39. Tan K.L., Chelvanaygam G., Parker, M.W., Board, P.G. Mutagenesis of the active site of the human Theta-class glutathione transferase GSTT2-2: catalysis with different substrates involves different residues. Biochem. J. 319:315-321, 1996.
40. Sherratt, P.J., Pulford, D.J., Harrison, D.J., Green. T., Hayes, J.D. Evidence that human class Theta glutathione S-transferase T1-1 can catalyse the activation of dichloromethane, a liver and lung carcinogen in the mouse. Biochem. J. 326:837-846, 1997.
41. Verschueren, K.H.G., Seljée, F., Rozeboom, H.J., Kalk, K.H., Dijkstra, B.W. Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase. Nature 363: 693-698, 1993.
42. Jemth. P., Stenberg, G., Chaga, G., Mannervik, B. Heterologous expression, purification, and characterization of rat class theta glutathione transferase T2-2. Biochem. J. 315:131-136, 1996.
43. Tan, K.L., Board, P.G. Purification and characterization of a recombinant human theta-class glutathione transferase (GSTT2-2) Biochem. J. 315:727-732, 1996.
44. Kabsch, W., Sander, C. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
45. Kraulis, P.J., MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-950, 1991.