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Pace H.C., Hodawadekar S.C., Draganescu A., Huang J., Bieganowski P., Pekarsky Y., Croce C.M., Brenner C. Crystal structure of the worm NitFhit Rosetta stone protein reveals a Nit tetramer binding two Fhit dimers. Curr Biol. 10:2000;907-917. This paper satisfied the phylogenetic profiles criterion [9] for Nit and Fhit as Rosetta stone proteins, defined the α-β-β-α protein fold and the Glu-Lys-Cys catalytic triad that are found throughout the nitrilase superfamily, and showed how Nit and Fhit fit together.
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Independent of [10••], this paper defined the α-β-β-α protein fold and the Glu-Lys-Cys catalytic triad that are found throughout the nitrilase superfamily.
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This paper classified the nitrilase superfamily into 13 branches, showing that only branch 1 contains nitrilases, whereas the other branches perform amide hydrolysis and condensation chemistry. Seven of the thirteen branches were functionally defined, in part, by the presence of Rosetta stone [7,8] fusions. In the most striking example, branches 7 and 8 were inferred to be glutaminases for associated NAD synthetase domains.
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