Fig. 3: Recognition of A35/U36 by the ABD of ScIleRS. | Nature Communications

Fig. 3: Recognition of A35/U36 by the ABD of ScIleRS.

From: The mechanism of discriminative aminoacylation by isoleucyl-tRNA synthetase based on wobble nucleotide recognition

Fig. 3

a Electrostatic surface potential of the positively charged cavity formed by the ABD, C-ter A, and C-ter C domains for binding the anticodon loop of tRNAIle(GAU). b Base-specific interactions between the anticodon loop of tRNAIle(GAU) and the ABD of ScIleRS. c As shown in the SaIleRS·tRNAIle(GAU)·mupirocin complex structure (PDB ID: 1FFY), the ABD of SaIleRS only forms base-specific interactions with A35 of tRNAIle(GAU). d Different conformations of the anticodon loop between SaIleRS-bound and ScIleRS-bound tRNAIle(GAU) molecules. The nucleotides U33, G34 and U36 in the SaIleRS-bound tRNAIle(GAU) clash with the C-ter C ___domain of ScIleRS.

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