Abstract
The structure of the holo enzyme shows that the four chemically identical sub-units are arranged with almost perfect 222 symmetry. There are indications, however, that the active centre regions might only be related in pairs.
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References
Velick, S. F., and Furfine, C., in The Enzymes (edit. by Boyer, P. D., Lardy, H., and Myrbäck, K.), 7, 243 (Academic Press, New York, 1963).
Allison, W. S., and Kaplan, N. O., J. Biol. Chem., 239, 2140 (1964).
Perham, R. N., and Harris, J. I., J. Mol. Biol., 7, 316 (1963).
Jones, G. M. T., and Harris, J. I., FEBS Lett., 22, 185 (1972).
Watson, H. C., and Banaszak, L. J., Nature, 204, 918 (1964).
Wassarman, P. M., and Watson, H. C., FEBS Lett., 18, 51 (1970).
Campbell, J. W., Duée, E., Hodgson, G., Mercer, W. D., Stammers, D. K., Wendell, P. L., Muirhead, H., and Watson, H. C., Cold Spring Harbor Symp. Quant. Biol., 36, 165 (1971).
Baranowski, T., and Wolny, M., Acta Biol. Med. Germ., 11, 651 (1963).
Racker, E., and Krimsky, I., Nature, 169, 1043 (1952).
Fox, J. B., and Dandliker, W. B., J. Biol. Chem., 221, 1005 (1956).
Gorjunov, A. I., and Andreeva, N. S., Molekul. Biolog., 1, 261 (1967)
Mathews, B. W., J. Mol. Biol., 33, 491 (1968).
Bokhoven, C., Schoone, J. C., and Bijvoet, J. B., Acta Cryst., 4, 275 (1951).
Green, D. W., Ingram, V. M., and Perutz, M. F., Proc. Roy. Soc., A, 225, 287 (1954).
Kendrew, J. C., Bodo, G., Dintzis, H. M., Parrish, R. G., Wyckoff, H. W., and Phillips, D. C., Nature, 181, 662 (1958).
Watson, H. C., Shotton, D. M., Cox, J. M., and Muirhead, H., Nature, 225, 806 (1970).
Lipscomb, W. N., Coppola, J. C., Hartsuck, J. A., Ludwig, M. L., Muirhead, H., Searl, J., and Steitz, J. A., J. Mol. Biol., 19, 423 (1966).
Blow, D. M., and Crick, F. H. C., Acta Cryst., 12, 794 (1959).
Wolny, M., Acta Biochim. Polon., 15, 137 (1968).
Adams, M. J., McPherson, A., Rossmann, M. G., Schevitz, R. W., and Wonacott, A. J., J. Mol. Biol., 51, 31 (1970).
Adams, M. J., Haas, D. J., Jeffery, B. A., McPherson, A., Mermall, H. L., Rossmann, M. G., Schevitz, R. W., and Wonacott, A. J., J. Mol. Biol., 41, 159 (1969).
Adams, M. J., Ford, G. C., Koekoek, R., Lentz, P. J., McPherson, A., Rossmann, M. G., Smiley, I. E., Schevitz, R. W., and Wonacott, A. J., Nature, 227, 1098 (1970).
Tsernoglou, D., Hill, E., and Banaszak, L. J., J. Mol. Biol. (in the press).
Conway, A., and Koshland, D. E., Biochemistry, 7, 4011 (1968).
Trentham, D. R., Biochem. J., 109, 603 (1968).
Bernhard, S. A., and MacQuarrie, R. A. (in the press).
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WATSON, H., DUÉE, E. & MERCER, W. Low Resolution Structure of Glyceraldehyde 3-Phosphate Dehydrogenase. Nature New Biology 240, 130–133 (1972). https://doi.org/10.1038/newbio240130a0
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DOI: https://doi.org/10.1038/newbio240130a0