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. Expand
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. Expand
The structure of dehydrogenases
Recent three-dimensional determinations of various dehydrogenase structures have shown some common architectural and chemical principles. This has provided insights into such diverse problems asExpand
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
The glycine-rich sequence of protein kinases: a multifunctional element.
The structure of the nucleotide-binding site differs from classical folds in the large family of protein kinases, the catalytic domain of which has one of the highest degrees of conservation among all known proteins. Expand
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 otherExpand
Structural rules for globular proteins.
  • G. Schulz
  • Chemistry, Medicine
  • Angewandte Chemie
  • 1977
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 featuresExpand
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 ofExpand
Structural and functional relationships between aminoacyl-tRNA synthetases.
  • D. Moras
  • Biology, Medicine
  • Trends in biochemical sciences
  • 1992
Aminoacyl-tRNA synthetases can be divided in two groups of equal size on the basis of differences in the structure of their active sites, based on structural data (amino acid sequences and tertiary structures), which can be rationalized in functional terms. Expand
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.Expand


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. Expand
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
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. Expand
Partial similarities between yeast and liver alcohol dehydrogenases.
  • H. Jörnvall
  • Biology, Medicine
  • 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. Expand
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 aExpand
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. Expand
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. Expand
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 andExpand
Amino Acid Sequences of Clostridium pasteurianum Flavodoxin
  • J. Fox, S. S. Smith, J. R. Brown
  • Medicine, Chemistry
  • Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie
  • 1972
The amino acid sequences of 10 tryptic peptides from C. pasteurianum flavodoxin are determined and ordered and new electrophoretic techniques for sequence determination are presented. Expand
Polypeptide conformation of cytoplasmic malate dehydrogenase from an electron density map at 3.0 Å resolution
Abstract The polypeptide chain conformation of both subunits of eytoplasmic malate dehydrogenase has been determined from an electron density map at 3.0 A resolution. The two polypeptide chains areExpand