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B6db references: 19608919

type Journal Article
authors Palioura S, Sherrer RL, Steitz TA, Söll D, Simonovic M.
title The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation
journal Science
Activity 2.9.1.2
Family 2.9.1.2
sel selected
ui 19608919
year (2009)
volume 325
number 5938
pages 321-5
 
abstract Selenocysteine is the only genetically encoded amino acid in humans whose biosynthesis occurs on its cognate transfer RNA (tRNA). O-Phosphoseryl-tRNA:selenocysteinyl-tRNA synthase (SepSecS) catalyzes the final step of selenocysteine formation by a poorly understood tRNA-dependent mechanism. The crystal structure of human tRNA(Sec) in complex with SepSecS, phosphoserine, and thiophosphate, together with in vivo and in vitro enzyme assays, supports a pyridoxal phosphate-dependent mechanism of Sec-tRNA(Sec) formation. Two tRNA(Sec) molecules, with a fold distinct from other canonical tRNAs, bind to each SepSecS tetramer through their 13-base pair acceptor-TPsiC arm (where Psi indicates pseudouridine). The tRNA binding is likely to induce a conformational change in the enzyme's active site that allows a phosphoserine covalently attached to tRNA(Sec), but not free phosphoserine, to be oriented properly for the reaction to occur.
last changed 2010/01/12 13:20

B6db references