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.
Abstract Atomic coordinates are presented for the 3740 atoms other than hydrogen in the dimeric molecule of chicken muscle triose phosphate isomerase. They are derived from an electron-density map atExpand
Crystallographic structure analysis of glucose 6-phosphate isomerase at 3-5 A resolution.
X-ray diffraction data sets have been measured from crystals of porcine skeletal muscle glucose 6-phosphate isomerase using a four-circle diffractometer and a Fourier map has been calculated and has been interpreted in terms of the folding of the polypeptide chain. Expand
The structure of proteins in aqueous solutions: an assessment of triose phosphate isomerase structure by Fourier-transform infrared spectroscopy.
The presence of beta-edge structure interacting with the alpha-helical barrel is described and discussed and measurements of band intensities, both in original and deconvolved spectra are shown to be unreliable for the quantification of secondary structures. Expand
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 substratesExpand
The double domain structure of rhodanese.
A 3 A electron density map of bovine liver rhodanese shows, in conjunction with gel electrophoresis experiments, that rhodanese consists of a single polypeptide chain with molecular weight of 32,000.Expand
A TIM barrel protein without enzymatic activity? Crystal‐structure of narbonin at 1.8 Å resolution
The first three dimensional crystal structure of a seed storage globulin at high resolution is reported, reporting the first protein with this topology possessing no known enzymatic activity from Vicia narbonensis L. Expand
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. Expand
Three-dimensional structure of cat muscle pyruvate kinase at 3·1 Å resolution
X-ray diffraction data sets have been collected by screened precession photography to a nominal resolution of 3·1 A from crystals of cat muscle pyruvate kinase. The films were processed using anExpand
The TIM barrel—the most frequently occurring folding motif in proteins
The TIM-barrel fold has now been found in 19 enzymes with different catalytic functions and different lengths of polypeptide chains, including the first examples of evolutionarily related enzymes that catalyze different chemical reactions. Expand
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 structureExpand


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. Expand
The amino acid sequence of rabbit muscle triose phosphate isomerase
The crystallographic remits on rabbit TIM showed it to be a dimer; the sub-units, related by a two-fold rotation axis, had a molecular weight o f 26,000 and the polypeptide chain has 248 amino acid residues, and it is found that the molecular weight of the dimer is 53,257. Expand
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 aloneExpand
Changes in absorption spectrum and crystal structure of triose phosphate isomerase brought about by 2-phosphoglycollate, a potential transition state analogue.
2-Phosphoglycollate, a strong inhibitor, alters the ultraviolet spectrum of triose phosphate isomerase, suggesting that the enzyme may undergo progressive changes from its native structure during substrate binding and catalysis. Expand
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. Expand
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. Expand
Conformation of twisted β-pleated sheets in proteins
Abstract It is shown that β-pleated sheets with a right-hand twist when viewed along the polypeptide chain direction have a lower free energy than sheets that are straight or which have a left-handExpand
Comparison of super-secondary structures in proteins.
The occurrence of larger continuous folds (“super-secondary structures”) has been detected in the comparison of lactate dehydrogenase with itself and with other protein structures. Expand
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. Expand
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.