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. Author manuscript; available in PMC: 2009 Apr 16.
Published in final edited form as: Nat Struct Mol Biol. 2008 Sep;15(9):990–997. doi: 10.1038/nsmb.1472

Figure 1.

Figure 1

Est3 is an OB-fold-containing protein with structural similarity to the OB-fold of TPP1. (a) Alignment of the proposed OB-fold domain of the Est3 protein; aa 16 to 173 of the 181 amino acid S. cerevisiae protein is shown. Black arrowheads indicate 3 invariant, or nearly invariant, residues that are common to the Est3 and TPP1 protein families, and white arrowheads indicate an additional 7 amino acids that appear to be conserved between the two proteins (see Supplementary Fig. 1 for an alignment of TPP1). The position of TPP1 secondary structure assignments38 are indicated (α helices and β strands, as cylinders and arrows, respectively), based on the structural comparison between Est3 and TPP1 shown in Fig. 1b; the C-terminal α helix (αC) present in TPP1 could not be detected in Est3. (b) A ribbon representation of the predicted structure of Est3 (aa 16 to 173, indicated in blue), overlaid with the structure of the OB-fold domain of TPP1 (aa 93 to 222, indicated in red).