Structure-function analysis of Sua5 protein reveals novel functional motifs required for the biosynthesis of the universal t⁶A tRNA modification.

ABSTRACT: N⁶-threonyl-carbamoyl adenosine (t⁶A) is a universal tRNA modification found at position 37, next to the anticodon, in almost all tRNAs decoding ANN codons (where N = A, U, G, or C). t⁶A stabilizes the codon-anticodon interaction and hence promotes translation fidelity. The first step of the biosynthesis of t⁶A, the production of threonyl-carbamoyl adenylate (TC-AMP), is catalyzed by the Sua5/TsaC family of enzymes. While TsaC is a single domain protein, Sua5 enzymes are composed of the TsaC-like domain, a linker and an extra domain called SUA5 of unknown function. In the present study, we report structure-function analysis of Pyrococcus abyssi Sua5 (Pa-Sua5). Crystallographic data revealed binding sites for bicarbonate subst

SUBMITTER: Pichard-Kostuch A 

PROVIDER: S-EPMC6004061 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature