Fig. 1: Biochemical and structural boundaries of N. gonorrhoeae LeuRS. | Communications Biology

Fig. 1: Biochemical and structural boundaries of N. gonorrhoeae LeuRS.

From: Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip

Fig. 1: Biochemical and structural boundaries of N. gonorrhoeae LeuRS.

a The enzymatic steps catalyzed by LeuRS. The first two stages occur in the aminoacylation domain (green box) while the post-transfer editing of mischarged Nva-tRNALeu is processed in the editing domain (cyan box). Nva is the abbreviation of non-canonical amino acid l-norvaline. b The domain structure of N. gonorrhoeae LeuRS and c its corresponding cartoon representation. The aminoacylation domain (green) is split by multiple insertions: connective polypeptide 1 (CP1 hairpin, purple) and 2 (CP2, slate); the editing domain (cyan); the zinc-binding domain (Zn2, yellow) and the leucine specific domain (LS, orange). The aminoacylation domain is followed by the anti-codon binding domain (ACBD, magenta) and the C-terminal domain (CTD, brown). A zinc ion is shown as a gray sphere.

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