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Figure 3.
Figure 3. Interactions of ProRSs with ATP
(A–C) Active
sites of (A) R. palustris, (B) E. faecalis, and (C) T.
thermophilus ProRS with bound ATP (predominantly pink molecule),
showing hydrogen bonds with key interacting residues. The
insertion domains are in magenta (in [A] and [B]), and the
eukaryote/archae-type-specific C-terminal domain is in yellow
(in [C]). Note the functionally equivalent roles of Glu218 in
PrsRp and PrsEf with the conserved carboxy terminus (Tyr477) in
PrsTt. In each case, the proline-binding loop is in the open
conformation.
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