|
Figure 2.
Figure 2. Oligonucleotide/Oligosaccharide–Binding (OB)
Folds within On TEBPThe four OB folds of On TEBP are shown in
the top row. Residue limits for each OB fold of On TEBP are
indicated and the labels are colored as in Figure 1: light
purple and dark purple for the two OB folds of the α N-terminal
domain, green for the α C-terminal domain, and blue for β. The
OB folds from the α N-terminal domain and β subunit each
interact with the single strand telomeric DNA, shown as a gray
stick model. The OB fold from the α C-terminal domain is shown
complexed with the extended peptide loop of the β subunit,
shown as a blue stick model. For comparison, the originally
described ( [32]) examples of the OB fold are shown in the
bottom row. These are the B subunit of verotoxin-1 from E. coli,
the anticodon-binding domain of aspartyl-tRNA synthetase
complexed with tRNA, staphylococcal nuclease complexed with the
Ca^2+-pTp inhibitor, and fd gene V protein. The strands and
loops of the OB fold are colored as follows: strand S1 in blue;
strand S2 in cyan; strand S3 in yellow; loop L[3–4] and the
intervening helix H, if present, in green; strand S4 in orange;
and strand S5 in red.
|
