Extended Data Fig. 5: Structural recognition of m-CF3-2-BMA (18) by MaFRSA and β7-β8 loop positioning in comparison with published PylRS structures. | Nature Chemistry

Extended Data Fig. 5: Structural recognition of m-CF3-2-BMA (18) by MaFRSA and β7-β8 loop positioning in comparison with published PylRS structures.

From: Expanding the substrate scope of pyrrolysyl-transfer RNA synthetase enzymes to include non-α-amino acids in vitro and in vivo

Extended Data Fig. 5: Structural recognition of m-CF3-2-BMA (18) by MaFRSA and β7-β8 loop positioning in comparison with published PylRS structures.The alternative text for this image may have been generated using AI.

a, Alignment of MmIFRS (N346S/C348Q, yellow, PDB: 4TQD) bound to 3-iodo-L-phenylalanine and AMP-PNP and MaFRSA bound to m-CF3-2-BMA (18) and AMP-PNP chain A (light purple) illustrating similar interactions between substrate carboxylate and backbone amides. b, The flexible β7-β8 loop ranges between unstructured, an open conformation, and a closed conformation across PylRS structures. MaFRSA bound to m-CF3-2-BMA and AMP-PNP (light purple), wild-type MaPylRS apo (green, PDB: 6JP2), wild-type MmPylRS bound to pyrrolysine and AMP-PNP (blue, PDB: 2ZCE), and wild-type MmPylRS bound to pyrrolysyl-adenylate (brown, PDB: 2Q7H). Chain A (light purple, c) exhibits lower B-factors in the β5-β6 loop than chain B (dark purple, d) indicated by dark blue and thin ribbon for lower B-factors and dark red and thick ribbon for higher B-factors.

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