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Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data

Nature volume 255, pages 609–614 (1975)Cite this article

Abstract

Each subunit of triose phosphate isomerase is composed of alternate segments of polypeptide chain in the α- and β-conformations that are arranged to form an inner cylinder of parallel-pleated sheet and a largely helical outer shell. Residues participating in the subunit interface and the active sites have been identified.

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Author information

Author notes

  1. C. I. Pogson: Department of Biology, University of Kent, Canterbury, Kent, formerly at Department of Biochemistry, University of Bristol, UK.

  2. P. H. Corran and S. G. Waley: Sir William Dunn School of Pathology, University of Oxford, Oxford OXL 3PS, UK.

Authors and Affiliations

  1. Laboratory of Molecular Biophysics, Department of Zoology, University of Oxford, Oxford, OX1 3PS, UK

    D. W. Banner, A. C. Bloomer, G. A. Petsko, D. C. Phillips, C. I. Pogson, I. A. Wilson, P. H. Corran, A. J. Furth, J. D. Milman, R. E. Offord, J. D. Priddle & S. G. Waley

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  1. D. W. Banner
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  2. A. C. Bloomer
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  3. G. A. Petsko
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  4. D. C. Phillips
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  5. C. I. Pogson
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  6. I. A. Wilson
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  7. P. H. Corran
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  8. A. J. Furth
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  9. J. D. Milman
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  10. R. E. Offord
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  11. J. D. Priddle
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  12. S. G. Waley
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Banner, D., Bloomer, A., Petsko, G. et al. Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data. Nature 255, 609–614 (1975). https://doi.org/10.1038/255609a0

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