PNNL

Abstract

We report on a number of proteins recently solved by NESG the Northeast Structural Genomics and other structural genomics consortia. The proteins considered in this study have very different sequences but they share a similar structural core, characterized by a five-stranded beta sheet and, in most cases, by one additional alpha helix. This core corresponds to the PUA domain-like architecture in the SCOP database that classifies proteins by their structural similarity. Using sequence and structure alignments, solvent accessible surface properties and genomic analysis, we characterize a group of domains with sequence and structure signatures distinctly differing from those found for the previously described PUA domain-like domains such as PUA proper or ASCH. We refer to these newly defined domains as EVE. Like several PUA domain-like domains, EVE may have retained the ability to bind RNA. However, both the available experimental and computational data suggests important differences in the biochemical and cellular function of EVE domains with respect to the others. This study of EVE and its relatives illustrates how the combination of structure and genomics creates new insights by connecting a cornucopia of structures and sequences that map to the same evolutionary potential.