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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
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