Reactivity of selenomethionine - Dents in the magic bullet?

Structure

Volumn 6, Issue 7, 1998, Pages 815-819

  Smith, Janet L ^a   Thompson, Andrew ^b  

^a PURDUE UNIVERSITY   (United States)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (France)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0032527715     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00083-5     Document Type: Article

References (20)

1. Hendrickson, W.A. (1985). Analysis of protein structure from diffraction measurement at multiple wavelengths. Trans. Am. Cryst. Assn. 21, 11-21.
2. Doublié, S. (1997). Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276, 523-530.
3. Shepherd, L. & Huber, R.E. (1969). Some chemical and biochemical properties of selenomethionine. Can. J. Biochem. 47, 877-881.
4. Hendrickson, W.A., Smith, J.L., Phizackerley, R.P. & Merritt, E.A. (1988). Crystallographic structure analysis of lamprey hemoglobin from anomalous dispersion of synchrotron radiation. Proteins 4, 77-88.
5. Zainal, H.A., LaCroix, D.E. & Wolf, W.R. (1996). Utilization of Chromatographic and spectroscopic techniques to study the oxidation kinetics of selenomethionine. Fresenius J. Anal. Chem. 356, 311-314.
6. Olivas, R.M., Quevauviller, P. & Donard, O.F.X. (1998). Long term stability of organic selenium species in aqueous solutions. Fresenius J. Anal. Chem. 360, 512-519.
7. Brot, N., Fliss, H., Coleman, T. & Weissbach, H. (1984). Enzymatic reduction of methionine sulfoxide residues in proteins and peptides. Methods Enzymol. 107, 352-360.
8. Klayman, D.L. & Günther, W.H.H. (1973). Organic Selenium Compounds: Their Chemistry and Biology. Wiley-lnterscience, New York.
9. Padmaja, S., Squadrito, G.L., Lemercier, J.N., Cueto, R. & Pryor, W.A. (1997). Peroxynitrite-mediated oxidation of D,L-selenomethionine-kinetics, mechanism and the role of carbon dioxide. Free Radical Biol. Med. 23, 917-926.
10. Beckman, J.S. (1996). In Nitric Oxide. Principles and Actions. (Lancaster, J., ed.), pp. 1-82, Academic Press, San Diego, CA.
11. Dyda, F., Hickman, A.B., Jenkins, T.M., Engelman, A., Craigie, R. & Davies, D.R. (1994). Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. Science 266, 1981-1986.
12. Wu, H., Lustbader, J.W., Liu, Y., Canfield, R.E. & Hendrickson, W.A. (1994). Structure of human chorionic gonadotrophin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein. Structure 2, 545-558.
13. Daniels, D.L., Cohen, A.R., Anderson, J.M. & Brünger, A.T. (1998). Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition. Nat. Struct. Biol. 5, 317-325.
14. Weston, S.A., et al., & Pauptit, R.A. (1998). Crystal structure of the anti-fungal target N-myristoyl transferase. Nat. Struct. Biol. 5, 213-221.
15. Assmann, A., Briviba, K. & Sies, H. (1998). Reduction of methionine seloxide to selenomethionine by glutathione. Arch. Biochem. Biophys. 349, 201-203.
16. Sies, H., Sharov, V.S., Klotz, L.-O. & Briviba, K. (1997). Glutathione peroxidase protects against peroxynitrite-mediated oxidations: a new function for selenoproteins as peroxynitrite reductase. J. Biol. Chem. 272, 27812-27817.
17. Tesmer, J.J.G., Klem, T.J., Deras, M.L., Davisson, V.J. & Smith, J.L. (1996). The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Nat. Struct. Biol. 3, 74-86.
18. Hubbard, S.J. & Argos, P. (1994). Cavities and packing at protein interfaces. Protein Sci. 3, 2194-2206.
19. Budisa, N., et al., & Huber, R. (1997). Bioincorporation of telluromethionine into proteins: a promising new approach for X-ray structure analysis of proteins. J. Mol. Biol. 270, 616-623.
20. Smith, J.L. (1997). Multiwavelength anomalous diffraction in macromolecular crystallography. In Recent Advances in Phasing. Proceedings of the CCP4 Study Weekend. (Wilson, K.S., Davies, G., Ashton, A.W. & Bailey, S., eds), pp. 25-39, CCLRC, Daresbury Laboratory, Warrington, UK.