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New structural and functional contexts of the Dx[DN]xDG linear motif: Insights into evolution of Calcium-binding proteinsстатья
Статья опубликована в высокорейтинговом журнале
Статья опубликована в журнале из списка Web of Science и/или Scopus- Авторы: Rigden D.J., Woodhead D.D., Wong P.W.H, Galperin M.Y.
- Журнал: PLoS ONE
- Том: 6
- Номер: 6
- Год издания: 2011
- Издательство: Public Library of Science
- Местоположение издательства: United States
- DOI: 10.1371/journal.pone.0021507
- Аннотация: Binding of calcium ions (Ca 2+) to proteins can have profound effects on their structure and function. Common roles of calcium binding include structure stabilization and regulation of activity. It is known that diverse families - EF-hands being one of at least twelve - use a Dx[DN]xDG linear motif to bind calcium in near-identical fashion. Here, four novel structural contexts for the motif are described. Existing experimental data for one of them, a thermophilic archaeal subtilisin, demonstrate for the first time a role for Dx[DN]xDG-bound calcium in protein folding. An integrin-like embedding of the motif in the blade of a ?-propeller fold - here named the calcium blade - is discovered in structures of bacterial and fungal proteins. Furthermore, sensitive database searches suggest a common origin for the calcium blade in ?-propeller structures of different sizes and a pan-kingdom distribution of these proteins. Factors favouring the multiple convergent evolution of the motif appear to include its general Asp-richness, the regular spacing of the Asp residues and the fact that change of Asp into Gly and vice versa can occur though a single nucleotide change. Among the known structural contexts for the Dx[DN]xDG motif, only the calcium blade and the EF-hand are currently found intracellularly in large numbers, perhaps because the higher extracellular concentration of Ca 2+ allows for easier fixing of newly evolved motifs that have acquired useful functions. The analysis presented here will inform ongoing efforts toward prediction of similar calcium-binding motifs from sequence information alone.
- Добавил в систему: Galperin Michael Y.