Structure-based experimental confirmation of biochemical function to a methyltransferase, MJ0882, from hyperthermophile Methanococcus jannaschii
Tóm tắt
We have determined the three-dimensional (3-D) structure of protein MJ0882, which derives from a hypothetical open reading frame in the genome of the hyperthermophile Methanococcus jannaschii. The 3-D fold of MJ0882 at 1.8 Å highly resembles that of a methyltransferase, despite limited sequence similarity to any confirmed methyltransferase. The structure has an S-adenosylmethionine (AdoMet) binding pocket surrounded by motifs with similarities to those commonly found among AdoMet binding proteins. Preliminary biochemical experiments show that MJ0882 specifically binds to AdoMet, which is the essential co-factor for methyltransferases.
Tài liệu tham khảo
Schluckebier, G., O'Gara, M., Saenger, W. and Cheng, X. (1995) J. Mol. Biol. 247, 16–20.
Cheng, X., Kumar, S., Posfai, J., Pflugrath, J.W. and Roberts, R.J. (1993) Cell 74, 299–307.
Klimasauskas, S., Kumar, S., Roberts, R.J. and Cheng, X. (1994) Cell 76, 357–369.
Labahn, J. et al. (1994) Proc. Natl. Acad. Sci. USA 91, 10957–10961.
Reinisch, K.M., Chen, L., Verdine, G.L. and Lipscomb, W.N. (1995) Cell 82, 143–153.
Gong, W., O'Gara, M., Blumenthal, R.M. and Cheng, X. (1997) Nucleic Acids Res 25, 2702-2715.
Vidgren, J., Svensson, L.A. and Liljas, A. (1994) Nature 368, 354–358.
Fu, Z. et al. (1996) Biochemistry 35, 11985–11993.
Hodel, A.E., Gershon, P.D., Shi, X. and Quiocho, F.A. (1996) Cell 85, 247–256.
Bussiere, D.E. et al. (1998) Biochemistry 37, 7103–7112.
Djordjevic, S. and Stock, A.M. (1997) Structure 5, 545–558.
Aravind, L. and Koonin, E.V. (2001) Trends Biochem. Sci. 26, 215–217.
Holm, L. and Sander, C. (1993) J. Mol. Biol. 233, 123–138.
Hendrickson, W.A. (1991) Science 254, 51-58.
Cheng, X. (1995) Annu. Rev. Biophys. Biomol. Struct. 24, 293–318.
Kim, R. et al. (1998) Biotech. Lett 20, 207-210.
Jancarik, J., Scott, W.G., Milligan, D.L., Koshland, D.E., Jr. and Kim, S.H. (1991) J. Mol. Biol. 221, 31-34.
Otwinowski, Z. and Minor, W. (1997) Methods Enzymol. 276, 307–326.
Terwilliger, T.C. (1997) Methods Enzymol. 276, 530.
Cowtan, K. and Main, P. (1998) Acta Crystallogr. D Biol. Crystallogr. 54, 487–493.
Jones, T.A., Zou, J.-Y., Cowan, S.W. and Kjeldgaard, M. (1991) Acta Crystallogr. A47, 110–119.
Brunger, A.T. et al. (1998) Acta Crystallogr. D54, 905–921.
Kraulis, P.J. (1991) J. Appl. Crystallogr. 24, 946–950.