Structural highlights
Function
[SELB_MOOTH] Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of the first two winged-helix motifs of translation elongation factor SelB from Moorella thermoacetica has been determined at 1.1 A resolution. Compared with the previous structure of the two domains in conjunction with winged-helix modules 3 and 4, the first winged-helix domain underwent a substantial conformational change during which the alpha-helical and beta-sheet portions of the element opened up like a shell. This conformational rearrangement was elicited by a change in the orientation of Trp396, leading to the disclosure of a bona fide ligand-binding site in the direct vicinity of Trp396. Additionally, the C-terminal tail of the second domain followed a different path compared with the previous structure. It is conceivable that these conformational switches constitute part of the molecular mechanism that underlies the communication between the N-terminal part of SelB, which binds Sec-tRNA(Sec) and GTP, and the C-terminal part of the protein, which binds selenocysteine-insertion sequences.
Conformational switches in winged-helix domains 1 and 2 of bacterial translation elongation factor SelB.,Ganichkin O, Wahl MC Acta Crystallogr D Biol Crystallogr. 2007 Oct;63(Pt 10):1075-81. Epub 2007, Sep 19. PMID:17881825[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ganichkin O, Wahl MC. Conformational switches in winged-helix domains 1 and 2 of bacterial translation elongation factor SelB. Acta Crystallogr D Biol Crystallogr. 2007 Oct;63(Pt 10):1075-81. Epub 2007, Sep 19. PMID:17881825 doi:10.1107/S0907444907042229
