5x6c
Crystal structure of SepRS-SepCysE from Methanocaldococcus jannaschiiCrystal structure of SepRS-SepCysE from Methanocaldococcus jannaschii
Structural highlights
FunctionSEPS_METJA Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).[1] Publication Abstract from PubMedCysteine 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) between SepRS and SepCysS distant active sites. This channeling mechanism could facilitate the consecutive reactions of the two-step indirect pathway of Cys-tRNA(Cys) synthesis (tRNA-dependent cysteine biosynthesis) to prevent challenge of translational fidelity, and may reflect the mechanism that cysteine was originally added into genetic code. Structural basis for tRNA-dependent cysteine biosynthesis.,Chen M, Kato K, Kubo Y, Tanaka Y, Liu Y, Long F, Whitman WB, Lill P, Gatsogiannis C, Raunser S, Shimizu N, Shinoda A, Nakamura A, Tanaka I, Yao M Nat Commun. 2017 Nov 15;8(1):1521. doi: 10.1038/s41467-017-01543-y. PMID:29142195[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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