Chemical and biological evolution of a nucleotide-binding protein

@article{Rossmann1974ChemicalAB,
  title={Chemical and biological evolution of a nucleotide-binding protein},
  author={Michael G. Rossmann and Dino Moras and Kenneth W Olsen},
  journal={Nature},
  year={1974},
  volume={250},
  pages={194-199}
}
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 would fail. Minimum base changes per codon can then be used to measure evolutionary distances which suggest that this structure was present during precellular evolution. 

Structural evidence for gene duplication in the evolution of the acid proteases

X-ray studies of acid proteases indicate a bilobal structure with a well defined active site cleft and a possible mechanism for evolution by gene duplication, divergence and gene fusion is presented.

The coenzyme-binding domains of glutamate dehydrogenases

Two coenzyme-binding domains are located in each of the sequences of bovine and Neurospora glutamate dehydrogenases and one domain shows significant sequence homology with the structurally-similar domain of glyceraldehyde-3-phosphate dehydrogenase.

Actin as an ancient nucleotide‐binding protein

In order to propose how actin may become energized by ATP, a three-dimensional structure of the nucleotide-binding domain of actin is constructed, based on homologous structures of other

Structural rules for globular proteins.

Is it possible to reach a detailed understanding of the complex three-dimensional structures of native polypeptide chains? In view of the wealth of common physicochemical and phylogenetic features

Structure of yeast phosphoglycerate mutase

A 3.5 Å resolution electron density map of yeast phosphoglycerate mutase has been calculated which shows that much of the tertiary structure of this enzyme resembles that found in a number of

Structural and functional relationships between aminoacyl-tRNA synthetases.

  • D. Moras
  • Chemistry, Biology
    Trends in biochemical sciences
  • 1992

The Nucleotide and Nucleotide-Like Coenzymes in Primitive Metabolism, Photobiology and Evolution

The evolutionary link between hypothetical primordial RNA world [1] and the modern R(D)NA/Protein biosphere can hardly be revealed by only searching for chemical roots of primitive genetic coding.
...

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