Chemical and biological evolution of a nucleotide-binding protein

  title={Chemical and biological evolution of a nucleotide-binding protein},
  author={Michael G. Rossmann and Dino Moras and Kenneth W Olsen},
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.

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

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.



Evolution of Enzyme Regulator Sites: Evidence for Partial Gene Duplication from Amino-acid Sequence of Bovine Glutamate Dehydrogenase

Some proteins, however, possess within individual subunits both active sites and regulatory sites capable of mediating homotropic and/or heterotropic interaction and the regulation of some oligomeric proteins, notably haemoglobin2.

Comparison of super-secondary structures in proteins.

Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster Muscle

Amino-acid sequence studies show that the active enzyme-NAD complex with a molecular weight of 146,000 is composed of four protein chains of identical sequence.

Partial similarities between yeast and liver alcohol dehydrogenases.

  • H. Jörnvall
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1973
The primary structure of about half of the protein chain of yeast alcohol dehydrogenase has been determined and compared with the amino-acid sequences of other dehydrogenases, and long segments within the N-terminal parts of the molecules are homologous, suggesting a common and important function for these segments.

Structure of Subtilisin BPN′ at 2.5 Å Resolution

The single polypeptide chain is folded into three parts, with the active site at their conjunction. In the active enzyme, the side chain of His 64 is in a position consistent with the formation of a

D-glyceraldehyde-3-phosphate dehydrogenase: three-dimensional structure and evolutionary significance.

The coenzyme binding portion of the enzyme has almost the same fold as the corresponding portion of lactate dehydrogenase, suggesting the presence of this structure in the five enzymes, analyzed so far, that use nucleotide coenzymes might indicate a fundamental primordial structural element.

Glyceraldehyde 3-Phosphate Dehydrogenase from Pig Muscle

A unique amino-acid sequence for the polypeptide chain of pig muscle glyceraldehyde 3-phosphate dehydrogenase has been derived and there is a striking homology between the sequence of this enzyme and that of the same enzyme from lobster—a phylogenetically distant organism.

Structure of Lactate Dehydrogenase at 2.8 Å Resolution

Electron density distributions for the M4 isoenzyme of LDH reveal details of the conformation of the subunit, boundaries between the subunits, and features relevant to the binding of coenzyme and

On the Evidence for Partial Gene Duplication from Amino Acid Sequence of Bovine Glutamate Dehydrogenase

It is shown that the observation quoted above is highly significant and that as there are 352 possible sequences of fifty residues with which section 114–163 may be aligned without overlapping itself the overall probability is 352×4.3×10−6.