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Figure 2.
Fig. 2. Structure of the dimeric human TrpRS with one
monomer shown in color. The circled CP1 insertion of the
Rossmann fold domain forms the dimerization interface. All three
domains [N-terminal appended domain (blue), Rossmann fold
catalytic domain (yellow), and anticodon recognition domain
(green)] were resolved in one monomer of the dimer with a
disordered linker of 21 residues connecting the N-domain and the
Rossmann fold domain. However, in the other monomer, the first
96 residues, which include the N-terminal domain, the linker
region, and part of the Rossmann fold catalytic domain, were
completely disordered. A bound Trp-AMP was found only in the
monomer with the resolved N-domain.
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