Abstract
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 language | English |
|---|---|
| Journal | Biochimie |
| Volume | 78 |
| Issue number | 11-12 |
| Pages (from-to) | 971-978 |
| Number of pages | 8 |
| ISSN | 0300-9084 |
| DOIs | |
| Publication status | Published - 1996 |
Funding
We thank H Schtitz for help with computer calculations. This work was supported by grants from the Deutsche Forschungsgemein- schaft (SFB 369), from the DESY-PS, 7rom European Commission via its Human Capital and Mobility Programme, and from the Fonds der Chemischen lndustrie.
Research Areas and Centers
- Academic Focus: Center for Infection and Inflammation Research (ZIEL)
