Methionyl-tRNA synthetase shows the nucleotide binding fold observed in dehydrogenases
- 1 July 1981
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 292 (5821) , 384-386
- https://doi.org/10.1038/292384a0
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Structure and control of phosphofructokinase from Bacillus stearothermophilusNature, 1979
- Crystallographic studies on the activity of glycogen phosphorylase bNature, 1978
- Structure of pyruvate kinase and similarities with other enzymes: possible implications for protein taxonomy and evolutionNature, 1978
- High resolution X-ray structure of yeast hexokinase, an allosteric protein exhibiting a non-symmetric arrangement of subunitsJournal of Molecular Biology, 1976
- Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolutionJournal of Molecular Biology, 1976
- Three-dimensional structure of d-glyceraldehyde-3-phosphate dehydrogenaseJournal of Molecular Biology, 1974
- Topological comparison of adenyl kinase with other proteinsNature, 1974
- Structure of horse muscle phosphoglycerate kinase: Some results on the chain conformation, substrate binding and evolution of the molecule from a 3 Å Fourier mapJournal of Molecular Biology, 1974
- Polypeptide conformation of cytoplasmic malate dehydrogenase from an electron density map at 3.0 Å resolutionJournal of Molecular Biology, 1972
- Structural Constraints of Possible Mechanisms of Lactate Dehydrogenase as Shown by High Resolution Studies of the Apoenzyme and a Variety of Enzyme ComplexesPublished by Cold Spring Harbor Laboratory ,1972