Advertisement

Journal of Biosciences

, Volume 12, Issue 1, pp 13–21 | Cite as

X-ray studies on crystalline complexes involving amino acids and peptides. Part XIV: Closed conformation and head-to-tail arrangement in a new crystal form of L-histidine L-aspartate monohydrate

  • C. G. Suresh
  • M. Vijayan
Article

Abstract

A new form of L-histidine L-aspartate monohydrate crystallizes in space group P22 witha = 5.131(1),b = 6.881(1),c= 18.277(2) Å,β= 97.26(1)° and Z = 2. The structure has been solved by the direct methods and refined to anR value of 0.044 for 1377 observed reflections. Both the amino acid molecules in the complex assume the energetically least favourable allowed conformation with the side chains staggered between the α-amino and α-scarboxylate groups. This results in characteristic distortions in some bond angles. The unlike molecules aggregate into alternating double layers with water molecules sandwiched between the two layers in the aspartate double layer. The molecules in each layer are arranged in a head-to-tail fashion. The aggregation pattern in the complex is fundamentally similar to that in other binary complexes involving commonly occurring L amino acids, although the molecules aggregate into single layers in them. The distribution of crystallographic (and local) symmetry elements in the old form of the complex is very different from that in the new form. So is the conformation of half the histidine molecules. Yet, the basic features of molecular aggregation, particularly the nature and the orientation of head-to-tail sequences, remain the same in both the forms. This supports the thesis that the characteristic aggregation patterns observed in crystal structures represent an intrinsic property of amino acid aggregation.

Keywords

Histidine aspartate complex crystal structure amino acid aggregation amino acid conformation chemical evolution 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Benedetti, E., Morelli, G., Nemethy, G. and Scheraga, H. A. (1983)Int. J. Peptide Protein Res.s 22, 1.CrossRefGoogle Scholar
  2. Bhat, T. N., Sasisekharan, V. and Vijayan, M. (1979)Int. J. Peptide Protein Res.,13, 170.CrossRefGoogle Scholar
  3. Bhat, T. N., Sudhakar, V. and Vijayan, M. (1980) inBiomolecular structure, conformation, function and evolution (ed. ′R. Srinivasan) (Oxford, New York: Pergamon Press) vol. 1, p. 633.Google Scholar
  4. Bhat, T. N. and Vijayan, M. (1976)Acta Crystallogr.,B32, 891.Google Scholar
  5. Bhat, T. N. and Vijayan, M. (1977)Acta Crystallogr.,B33, 1754.Google Scholar
  6. Bhat, T. N. and Vijayan, M. (1978)Acta Crystallogr.,B34, 2556.Google Scholar
  7. Germain, G., Main, P. and Woolfson, M. M. (4971)Acta Crystallogr.,A27, 368.Google Scholar
  8. Hamilton, W. C. (1959)Acta Crystallogr.,12, 609.CrossRefGoogle Scholar
  9. IUPAC-IUB Commission on Biochemical Nomenclature (1970)J. Mol. Biol.,52, 1.CrossRefGoogle Scholar
  10. Janin, J., Wodak, S., Levitt, M. and Maigret, B. (1978)J. Mol. Biol.,125, 357.PubMedCrossRefGoogle Scholar
  11. Marsh, R. E. and Donohue, J. (1967) inAdvances in Protein Chemistry (eds C.′B. Anfinsen Jr., M. L. Anson, J. T. Edsall and F. M. Richards) (New York, London: Academic Press) vol.22, p. 235.Google Scholar
  12. Oda, K. and Koyama, H. (1972)Acta Crystallogr.,B28, 639.Google Scholar
  13. Ponnuswamy, P. K. and Sasisekharan, V. (1971)Int. J. Protein Res.,3, 9.PubMedGoogle Scholar
  14. Ramani, R. and Boyd, R. J. (1981)Can. J. Chem.,59, 3232.CrossRefGoogle Scholar
  15. Salunke, D. M. and Vijayan, M. (1982)Acta Crystallogr.,B38, 1328.Google Scholar
  16. Salunke, D. M. and Vijayan, M. (1983)Int. J. Peptide Protein Res.,22, 154.CrossRefGoogle Scholar
  17. Salunke, D. M. and Vijayan, M. (1984)Biochim. Biophys. Acta,798, 175.Google Scholar
  18. Sheldrick, G. M. (1976)SHELX 76. Program for crystal structure determination and refinement, University of Cambridge, England.Google Scholar
  19. Suresh, C. G., Jayanthi Ramaswamy and Vijayan, M. (1986)Acta Crystallogr.,B42, 473.Google Scholar
  20. Suresh, C. G. and Vijayan, M. (1983a)Int. J. Peptide Protein Res.,21, 223.CrossRefGoogle Scholar
  21. Suresh, C. G. and Vijayan, M. (1983b)Int. J. Peptide Protein Res.,22, 129.CrossRefGoogle Scholar
  22. Suresh, C. G. and Vijayan, M. (1983c)Int. J. Peptide Protein Res.,22, 617.CrossRefGoogle Scholar
  23. Suresh, C. G. and Vijayan, M. (1985a)Int. J. Peptide Protein Res.,26, 311.CrossRefGoogle Scholar
  24. Suresh, C. G. and Vijayan, M. (1985b)Int. J. Peptide Protein Res.,26, 329.CrossRefGoogle Scholar
  25. Vijayan, M. (1980)FEBS Lett.,112, 135.PubMedCrossRefGoogle Scholar
  26. Vijayan, M. (1983) inConformation in biology (eds R. Srinivasan and R. H. Sarma) (New York: Adenine Press) p. 175.Google Scholar
  27. Vijayan, M. and Suresh, C. G. (1985)Curr. Sci.,54, 771.Google Scholar

Copyright information

© Printed in India 1987

Authors and Affiliations

  • C. G. Suresh
    • 1
  • M. Vijayan
    • 1
  1. 1.Molecular Biophysics UnitIndian Institute of ScienceBangaloreIndia

Personalised recommendations