Abstract
A three-dimensional X-ray study at a resolution of 2.8 Å has revealed that the single polypeptide chain of 211 residues is folded into two distinct parts which are divided by a cleft. The active site, consisting of a cysteine and a histidine, lies at the surface of the cleft. Apart from four short α-helical segments and one short segment of β-structure, the conformation of the chain is irregular.
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References
Drenth, J., Jansonius, J. N., Koekoek, R., Marrink, J., Munnik, J., and Wolthers, B. G., J. Mol. Biol., 5, 398 (1962).
Light, A., Frater, R., Kimmel, J. R., and Smith, E. L., Proc. US Nat. Acad. Sci., 52, 1276 (1964).
Drenth, J., Jansonius, J. N., and Wolthers, B. G., J. Mol. Biol., 24, 449 (1967).
Drenth, J., Kloosterman, D., v.d. Woude, J., Croon, H. C., and v. Zwet, L. C. M., J. Sci. Instrum., 42, 222 (1965).
Phillips, D. C., J. Sci. Instrum., 41, 123 (1964).
Arndt, U. W., North, A. C. T., and Phillips, D. C., J. Sci. Instrum., 41, 421 (1964).
Blow, D. M., and Crick, F. H. C., Acta Cryst., 12, 794 (1959).
Dickerson, R. E., Kendrew, J. C., and Strandberg, B. E., Acta Cryst., 14, 1188 (1961).
North, A. C. T., Acta Cryst., 18, 212 (1965).
Matthews, B. W., Acta Cryst., 20, 82 (1966).
Schechter, I., and Berger, A., Biochem. Biophys. Res. Commun., 27, 157 (1967).
Sluyterman, L. A. A. E., Biochim. Biophys. Acta, 139, 418 (1967).
Lowe, G., and Williams, A., Biochem. J., 96, 194 (1965).
Husain, S. S., and Lowe, G., Chem. Commun., 310 (1968).
Shinitzky, N., and Goldman, R., Eur. J. Biochem., 3, 139 (1967).
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DRENTH, J., JANSONIUS, J., KOEKOEK, R. et al. Structure of Papain. Nature 218, 929–932 (1968). https://doi.org/10.1038/218929a0
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DOI: https://doi.org/10.1038/218929a0
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