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

@article{Banner1975StructureOC,
  title={Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data},
  author={David W. Banner and Anne C. Bloomer and Gregory A. Petsko and David C. Phillips and Christopher I. Pogson and Ian A. Wilson and Patrick H. Corran and Anna J. Furth and J. D. Milman and Robin Ewart Offord and John D. Priddle and Stephen G. Waley},
  journal={Nature},
  year={1975},
  volume={255},
  pages={609-614}
}
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. 

Atomic coordinates for triose phosphate isomerase from chicken muscle.

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The structure determination of pyruvate kinase shows that each subunit of the tetrameric molecule consists of three domains. The largest of these domains has a remarkable similarity to the structure

Primary structure of triosephosphate isomerase from Bacillus stearothermophilus.

Correlation of the sequence of the thermophile enzyme with the three-dimensional structure of the muscle enzyme shows that residues in the catalytic site and in the subunit interface are strongly conserved.
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