Abstract
A striking common structural feature has emerged from the comparison of the X-ray crystallographic studies of several dehydrogenases. In lactate dehydrogenase1, soluble malate dehydrogenase2, alcohol dehydrogenase3 and glyceraldehyde-3-phosphate dehydrogenase4 similar foldings have been described in the region which binds the coenzyme NAD, whereas no significant similarities were observed in the chemical sequences. The occurrence of a characteristic ‘nucleotide binding fold’ (the so-called Rossmann fold) has also been observed in horse muscle phosphoglycerate kinase5, in phosphorylase6,7 and, with some topological deviations, in other kinases8–11 as well as in the flavin-binding domain of flavodoxin12. If one assumes that these structural homologies are the result of a divergent evolutionary process, it is then tempting to predict a similar pattern of structure–function relationship in other nucleotide-binding proteins, in particular in aminoacyl-tRNA synthetases. We show here that methionyl-tRNA synthetase does show the same nucleotide binding fold.
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Risler, J., Zelwer, C. & Brunie, S. Methionyl-tRNA synthetase shows the nucleotide binding fold observed in dehydrogenases. Nature 292, 384–386 (1981). https://doi.org/10.1038/292384a0
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DOI: https://doi.org/10.1038/292384a0
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