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Structural genomics reveals EVE as a new ASCH/PUA‐related domain
Author(s) -
Bertonati Claudia,
Punta Marco,
Fischer Markus,
Yachdav Guy,
Forouhar Farhad,
Zhou Weihong,
Kuzin Alexander P.,
Seetharaman Jayaraman,
Abashidze Mariam,
Ramelot Theresa A.,
Kennedy Michael A.,
Cort John R.,
Belachew Adam,
Hunt John F.,
Tong Liang,
Montelione Gaetano T.,
Rost Burkhard
Publication year - 2008
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.22287
Subject(s) - structural genomics , genomics , domain (mathematical analysis) , computational biology , function (biology) , functional genomics , sequence (biology) , protein domain , biology , protein structure , genetics , genome , gene , biochemistry , mathematical analysis , mathematics
We report on several proteins recently solved by structural genomics consortia, in particular by the Northeast Structural Genomics consortium (NESG). The proteins considered in this study differ substantially in their sequences but they share a similar structural core, characterized by a pseudobarrel five‐stranded beta sheet. This core corresponds to the PUA domain‐like architecture in the SCOP database. By connecting sequence information with structural knowledge, we characterize a new subgroup of these proteins that we propose to be distinctly different from previously described PUA domain‐like domains such as PUA proper or ASCH. We refer to these newly defined domains as EVE . Although EVE may have retained the ability of PUA domains to bind RNA, the available experimental and computational data suggests that both the details of its molecular function and its cellular function differ from those of other PUA domain‐like domains. This study of EVE and its relatives illustrates how the combination of structure and genomics creates new insights by connecting a cornucopia of structures that map to the same evolutionary potential. Primary sequence information alone would have not been sufficient to reveal these evolutionary links. Proteins 2009. © 2008 Wiley‐Liss, Inc.