Structural model for the selenocysteine-specific elongation factor SelB

R. Hilgenfeld, A. Böck, R. Wilting*

*Corresponding author for this work
24 Citations (Scopus)


A structural model was established for the N-terminal part of translation factor SelB which shares sequence similarity with EF-Tu, taking into account the coordinates of the EF-Tu 3D structure and the consensus of SelB sequences from four bacteria. The model showed that SelB is homologous in its N-terminal domains over all three domains of EF-Tu. The guanine nucleotide binding site and the residues involved in GTP hydrolysis are similar to those of EF-Tu, but with some subtle differences possibly responsible for the higher affinity of SelB for GTP compared to GDP. In accordance, the EF-Tu epitopes interacting with EF-Ts are lacking in SelB. Information on the formation of the selenocysteyl-binding pocket is presented. A phylogenetic comparison of the SelB domains homologous to EF-Tu with those from EF-Tu and initiation factor 2 indicated that SelB forms a separate class of translation factors.

Original languageEnglish
Issue number11-12
Pages (from-to)971-978
Number of pages8
Publication statusPublished - 1996

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


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