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

  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},
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.

Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme

The fitting of sequenced peptides to a high-resolution X-ray map of phosphoglycerate kinase has yielded the complete sequence and structure of the horse muscle enzyme. Metal ADP and ATP substrates

Structure of yeast triosephosphate isomerase at 1.9-A resolution.

Analysis of the subunit interface of this dimeric enzyme hints at the source of the specificity of one subunit for another and allows us to estimate an association constant of 10(14)-10(16) M-1 for the two monomers, which suggests that the interface may be a particularly good target for drug design.

Structure of pyruvate kinase and similarities with other enzymes: possible implications for protein taxonomy and evolution

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.



Studies on the subunit structure and amino acid sequence of trisoe phosphate isomerase from chicken breast muscle.

Triose phosphate isomerase was prepared by chromatography on DEAE-cellulose of an (NH(4))(2)SO(4) fraction of an extract of homogenized chicken breast muscle, which is suitable for growing crystals for X-ray work.

Chemical and biological evolution of a nucleotide-binding protein

Three-dimensional alignment of the common nucleotide binding structure in dehydrogenases, kinases and flavodoxins permits the recognition of homologous amino acids when sequence comparisons alone

The active centre of rabbit muscle triose phosphate isomerase. The site that is labelled by glycidol phosphate.

The site of attachment of Glycidol (2,3-epoxypropanol) phosphate is studied and the glutamic acid residue in this peptide that is labelled is thus a gamma-glutamyl ester derived from glycerol phosphoric acid.

Triose phosphate isomerase from the coelacanth. An approach to the rapid determination of an amino acid sequence with small amounts of material.

Combination with results from manual sequence analysis has given the 247-residue amino acid sequence of coelacanth triose phosphate isomerase in 4 months, by using 100mg of enzyme.

Comparison of super-secondary structures in proteins.

Active-site labelling of triose phosphate isomerase. The reaction of bromohydroxyacetone phosphate with a unique glutamic acid residue and the migration of the label to tyrosine.

The failure of this reagent specifically to inactivate either muscle or yeast aldolase, and the use of the reagent in preparing isomerase-free glycolytic enzymes, is discussed.

A low‐temperature device for protein crystallography

A low-temperature device for use in the X-ray structural study of proteins has been designed and tested. It is easy to construct, portable, inexpensive to operate and extremely reliable in operation.