The crystal structure of human cytosolic serine hydroxymethyltransferase: A target for cancer chemotherapy

Structure

Volumn 6, Issue 9, 1998, Pages 1105-1116

  Renwick, Suzanne B ^a,b   Snell, Keith ^a   Baumann, Ulrich ^a,c  

^a INSTITUTE OF CANCER RESEARCH   (United Kingdom)

^b UCB PHARMA   (Belgium)

^c UNIVERSITY OF BERN   (Switzerland)

Author keywords

Cancer chemotherapy; Pyridoxal phosphate enzymes; Serine hydroxymethyltransferase; X ray crystallography

Indexed keywords

EUKARYOTA; PROKARYOTA;

EID: 0032530853     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00112-9     Document Type: Article

References (62)

1. Alexander, F.W., Sandmeier, E., Mehta, P.K. & Christen, P. (1994). Evolutionary relationships among pyridoxal-5′-phosphate-dependent enzymes. Eur. J. Biochem. 219, 953-960.
2. Schirch, L. (1984). Folates in serine and glycine metabolism. In Folates and Pterins: Chemistry and Biochemistry of Folates. (Blakely, R.L. & Benkovic, S.J. eds.), pp. 399-412, Wiley-lnterscience, New York, USA.
3. Thorndike, J., Pelliniemi, T.T. & Beck, W.S. (1979). Serine hydroxymethyltransferase activity and serine incorporation in leukocytes. Cancer Res. 39, 3435-3440.
4. Snell, K., Natsumeda, Y., Eble, J.N., Glover, J.L. & Weber, G. (1988). Enzymic imbalance in serine metabolism in human colon carcinoma and rat sarcoma. Br. J. Cancer. 57, 87-90.
5. Bukin, Y.V. & Draudin-Krylenko, V.A. (1980). Regulation of serine hydroxymethyltransferase activity in normal, tumour and host cells. Vest. Akad. Med. Nauk. SSSR 6, 67-69.
6. Snell, K. (1985). Enzymes of serine metabolism in normal and neoplastic rat tissues. Biochem. Biophys. Acta 843, 276-281.
7. Snell, K. & Weber, G. (1986). Enzymic imbalance in serine metabolism in rat hepatomas. Biochem. J. 233, 617-620.
8. Snell, K. & Riches, D. (1989). Effects of a triazine antifolate (NSC 127755) on serine hydroxymethyltransferase in myeloma cells in culture. Cancer Lett. 44, 217-220.
9. Filman, D.J., Bolin, J.T., Matthews, D.A. & Kraut, J. (1982). Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined to 1.7 Å resolution. II. Environment of bound NADPH and implications for catalysis. J. Biol. Chem. 257, 13663-13672.
10. Oefner, C., D'Arcy, A. & Winkler, F.K. (1988). Crystal structure of human dihydrofolate reductase complexed with folate. Eur. J. Biochem. 174, 377-385.
11. Hardy, L.W., Finer-Moore, J.S., Montfort, W.R., Jones, M.O., Santi, D.V. & Stroud, R.M. (1987). Atomic structure of thymidylate synthase: target for rational drug design. Science 235, 448-455.
12. Schiffer, C.A., Clifton, I.J., Davisson, V.J., Santi, D.V. & Stroud, R.M. (1995). Crystal structure of human thymidylate synthase: a structural mechanism for guiding substrates into the active site. Biochemistry 34, 16279-16287.
13. Huennekens, F.M. (1994). The methotrexate story: a paradigm for development of cancer chemotherapeutic agents. Adv. Enz. Regul. 34, 397-419.
14. Rustum, Y.M., et al., & Seeber, S. (1997). Thymidylate synthase inhibitors in cancer therapy: direct and indirect inhibitors. J. Clin. Oncol. 15, 389-400.
15. Hartman, P.G. (1993). Molecular aspects and mechanism of action of dihydrofolate reductase inhibitors. J. Chemother. 5, 369-376.
16. Then, R.L. (1993). History and future of antimicrobial diaminopyrimidines. J. Chemother. 5, 361-368.
17. Costi, M.P. (1998). Thymidylate synthase inhibition: a structure-based rationale for drug design. Med. Res. Rev. 18, 21-42.
18. Angelaccio, S., Pascarella, S., Fattori, E., Bossa, F., Strong, W. & Schirch, V. (1992). Serine hydroxymethyltransferase: origin of substrate specificity. Biochemistry 31, 155-162.
19. Stover, P., Zamora, M., Shostak, K., Gautam-Basak, M. & Schirch, V. (1992). Escherichia coli serine hydroxymethyltransferase: the role of histidine 228 in determining reaction specificity. J. Biol. Chem. 267, 17679-17687.
20. Schirch, D., et al., & Schirch, V. (1993). Function of the active-site lysine in Escherichia coli serine hydroxymethyltransferase. J. Biol. Chem. 268, 23132-23138.
21. Delle Fratte, S., Iurescia, S., Angelaccio, S., Bossa, F. & Schirch, V. (1994). The function of arginine 363 as the substrate carboxyl-binding site in Escherichia coli serine hydroxymethyltransferase. Eur. J. Biochem. 225, 395-401.
22. Cai, K. & Schirch, V. (1996). Structural studies on folding intermediates of serine hydroxymethyltransferase using fluorescence resonance energy transfer. J. Biol. Chem. 271, 27311-27320.
23. Usha, R., Savithri, H.S. & Rao, N.A. (1992). Arginine residues involved in binding of tetrahydrofolate to sheep liver serine hydroxymethyltransferase. J. Biol. Chem. 267, 9289-9293.
24. Jagath, J.R., Sharma, B., Rao, N.A. & Savithri, H.S. (1997). The role of His 134, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase. J. Biol. Chem. 272, 24355-24362.
25. Stover, P., Kruschwitz, H., Schirch, V. & Wright, H.T. (1993). Diffraction grade crystals of Escherichia coli serine hydroxymethyltransferase. J. Mol. Biol. 230, 1094-1096.
26. Sippl, M.J. (1993). Recognition of errors in three-dimensional structures of proteins. Proteins 17, 355-362.
27. Kleywegt, G.J. & Jones, T.A. (1996). Phi/Psi-chology: Ramachandran revisited. Structure 4, 1395-1400.
28. Kirsch, J.F., Eichele, G., Ford, G.C., Vincent, M.G. & Jansonius, J.N. (1984). Mechanism of the action of aspartate aminotransferase on the basis of its spatial structure. J. Mol. Biol. 174, 497-525.
29. Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 223, 123-138.
30. Antson, A.A., et al., & Wilson, K.S. (1993). Three-dimensional structure of tyrosine phenol-lyase. Biochemistry 32, 4195-4206.
31. Toney, M.D., Hohenester, E., Cowan, S.W. & Jansonius, J.N. (1993). Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites. Science 261, 756-759.
32. Toney, M.D., Hohenester, E., Keller, J.W. & Jansonius, J.N. (1995). Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate dependent enzyme dialkylglycine decarboxylase. J. Mol. Biol. 245, 151-179.
33. McPhalen, C.A., Vincent, M.G. & Jansonius, J.N. (1992). X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase. J. Mol. Biol. 225, 495-517.
34. Momay, C., Ernst, S., Ghosh, R. & Hackert, M.L. (1995). Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a. J. Mol. Biol. 252, 643-655.
35. Watanabe, N., et al., & Fukutani, H. (1989). Crystal structure of ω-amino acid: pyruvate aminotransferase with a newly developed Weissenberg camera and an imaging plate using synchrotron radiation. J. Biochem. 105, 1-3.
36. Clausen, T., Huber, R., Laber, B., Pohlenz, H.D. & Messerschmidt, A. (1996). Crystal structure of the pyridoxal-5′-phosphate dependent cystathionine β-lyase from Escherichia coli at 1.83 Å. J. Mol. Biol. 262, 202-224.
37. Richardson, J.S. (1981). The taxonomy and anatomy of protein structures. Adv. Protein Chem. 34, 167-333.
38. Mansouri, A., Decter, J.B. & Silber, R. (1972). Studies on the regulation of one-carbon metabolism. J. Biol. Chem. 247, 348-352.
39. Jagath, J.R., Sharma, B., Bhaskar, B., Datta, A., Rao, N.A. & Savithri, H.S. (1997). Importance of the amino terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase. Eur. J. Biochem. 247, 372-379.
40. Jordan, P.M. & Akhtar, M. (1970). The mechanism of action of serine transhydroxymethylase. Biochem. J. 116, 277-286.
41. Matthews, R.G. & Drummond, J.T. (1990). Providing one-carbon units for biological methylations: mechanistic studies on serine hydroxymethyltransferase, methylenetetrahydrofolate reductase, and methyltetrahydrofolate-homocysteine methyltransferase. Chem. Rev. 90, 1275-1290.
42. Toney, M.D. & Kirsh, J.F. (1993). Lysine 258 in aspartate aminotransferase: enforcer of the Circe effect for amino acid substrates and general-base catalyst for the 1,3-prototropic shift. Biochemistry 32, 1471-1479.
43. Renwick, S.B., Skelly, J.V., Chave, K.J., Sanders, P.G., Snell, K. & Baumann, U. (1998). The purification, crystallization and preliminary X-ray analysis of human recombinant cytosolic serine hydroxymethyltransferase. Acta Cryst. D, in press.
44. Jancarik, J. & Kim, S.H. (1991). Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Cryst. 24, 409-411.
45. Otwinowski, Z. & Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
46. Dirr, H., Reinemer, P. & Huber, R. (1994). Refined crystal structure of porcine class Pi glutathione S-transferase (pGST P1-1) at 2.1 Å resolution. J. Mol. Biol. 243, 72-92.
47. Doublié, S. & Carter, C.W. Jr. (1992). Preparation of selenomethionyl protein crystals. In Crystallisation of Nucleic Acids and Proteins: A Practical Approach. (Ducruix, A. & Giege, R. eds), pp. 311-317, IRL Press/Oxford University Press, Oxford, UK.
48. Rould, M.A. (1997). Screening for heavy-atom derivatives and obtaining accurate isomorphous differences. Methods Enzymol. 276, 461-472.
49. Sheldrick, G.M. (1997). Patterson superposition and ab initio phasing. Methods Enzymol. 276, 628-641.
50. CCP4 Collaborative Computational Project, Number 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
51. Otwinowski, Z. (1991). Isomorphous Replacement and Anomalous Scattering. In Proceedings of the Daresbury Study Weekend. pp. 80-85, SERC Daresbury Laboratory, Warrington, UK.
52. De La Fortelle, E. & Bricogne, G. (1997). Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494.
53. 1 ATPase. Acta Cryst. D 52, 30-42.
54. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
55. Kleywegt, G.J. & Jones, T.A. (1997). Detecting folding motifs and similarities in protein structures. Methods Enzymol. 277, 525-546.
56. Rice, L.M. & Brünger, AT. (1994). Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinement. Proteins 19, 277-290.
57. Brünger, A.T. (1992). X-PLOR, a System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT, USA.
58. Murshudov, G., Vagin, A. & Dodson, E.J. (1997). Refinement of macromolecular structures by the maximum entropy method. Acta Cryst D 53, 240-255.
59. Brünger, A.T. (1992). The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474.
60. Diederichs, K. & Karplus, P.A. (1997). Improved R-factors for diffraction analysis in macromolecular crystallography. Nat. Struct. Biol. 4, 269-275.
61. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
62. Merrit. E.A. & Bacon, D.J. (1997). Raster3D photorealistic molecular graphics. Methods Enzymol. 277, 505-524.