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Selenocysteine-specific elongation factor, winged helix domain
This domain is found in Selenocysteine-specific elongation factor from Escherichia coli (SelB) and similar bacterial sequences. SelB is a translation factor necessary for the incorporation of selenocysteine into proteins. The C-terminal region of this protein in bacteria shows four winged-helix (WH) domains arranged in tandem, which form two globular structures. This entry represents the second pair of WH domains (WH3 and 4). Each WH domain is an alpha-beta structure consisting of three alpha-helices and a twisted three- stranded antiparallel beta-sheet [1-3]. Paper describing PDB structure 1lva. [1]. 12145214. Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB. Selmer M, Su XD;. EMBO J. 2002;21:4145-4153. Paper describing PDB structure 1wsu. [2]. 15665870. Structural basis for mRNA recognition by elongation factor SelB. Yoshizawa S, Rasubala L, Ose T, Kohda D, Fourmy D, Maenaka K;. Nat Struct Mol Biol. 2005;12:198-203. Paper describing PDB structure 2pjp. [3]. 17537456. Structural insight into a molecular switch in tandem winged-helix motifs from elongation factor SelB. Soler N, Fourmy D, Yoshizawa S;. J Mol Biol. 2007;370:728-741. (from Pfam)
SelB C-terminal domain-containing protein
Members of this family adopt a winged-helix fold, with an alpha/beta structure consisting of three alpha-helices and a twisted three-stranded antiparallel beta-sheet, with an alpha-beta-alpha-alpha-beta-beta connectivity. They are involved in both DNA and RNA binding [1]. [1]. 12145214. Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB. Selmer M, Su XD;. EMBO J. 2002;21:4145-4153. (from Pfam)
DNA/RNA-binding winged helix domain-containing protein
GTP-binding protein
This domain contains a P-loop motif, also found in several other families such as Pfam:PF00071, Pfam:PF00025 and Pfam:PF00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains. Cryoelectron microscopy structure. [1]. 9311785. Visualization of elongation factor Tu on the Escherichia coli ribosome. Stark H, Rodnina MV, Rinke-Appel J, Brimacombe R, Wintermeyer W, van Heel M;. Nature 1997;389:403-406. (from Pfam)
selenocysteine-specific translation elongation factor
In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This HMM describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes.
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