Figure 1. Comparison of the modular organization of the subclass IIb aminoacyl-tRNA synthetases.

Figure 1

Comparison of the modular organization of the subclass IIb aminoacyl-tRNA synthetases. A-3D structures of T. thermophilus Asn-, Lys- and yeast AspRS. The upper and the lower modules represent respectively the catalytic and the anticodon-binding domains; the three class defining motifs are in black. The axes represent the angular deviations of the anticodon-binding domains with respect to the catalytic cores which were superimposed. B-Top view of the anticodon-binding domains. The angles formed by the anticodon-binding domain with the catalytic core were determined from axes joining two residues spatially conserved in the anticodon-binding domains (Phe42 and Val48 for AsnRS, Arg80 and Gln86 for LysRS, and Ile136 and Lys142 for AspRS) and their shift expressed by comparison with LysRS.

From: Asparaginyl-tRNA Synthetases

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