Structural basis for tRNA-dependent cysteine biosynthesis.

ABSTRACT: Cysteine can be synthesized by tRNA-dependent mechanism using a two-step indirect pathway, where O-phosphoseryl-tRNA synthetase (SepRS) catalyzes the ligation of a mismatching O-phosphoserine (Sep) to tRNA^Cys followed by the conversion of tRNA-bounded Sep into cysteine by Sep-tRNA:Cys-tRNA synthase (SepCysS). In ancestral methanogens, a third protein SepCysE forms a bridge between the two enzymes to create a ternary complex named the transsulfursome. By combination of X-ray crystallography, SAXS and EM, together with biochemical evidences, here we show that the three domains of SepCysE each bind SepRS, SepCysS, and tRNA^Cys, respectively, which mediates the dynamic architecture of the transsulfursome and thus enables a global long-range channeling of tRNA^Cys

SUBMITTER: Chen M 

PROVIDER: S-EPMC5688128 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature