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Figure 4.
Figure 4. Interactions of ProRSs with the Prolyl-Adenylate
Analog, ProAMS
(A–C) ProAMS (predominantly gray molecule)
bound in the active sites of (A) R. palustris, (B) E. faecalis,
and (C) T. thermophilus ProRS, showing key hydrogen bonds to the
proline and sulfate moieties. Class II synthetase conserved
motifs 1, 2, and 3 are shown in green, cyan, and red,
respectively, and the TXE loop is shown in gold. On the
proline-binding loop (violet), which is in the closed
conformation, hydrophobic residues Ile202, Met202, and Phe205
play equivalent roles in PrsRp, PrsEf, and PrsTt, respectively.
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