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- W2912786480 abstract "Abstract The Elongator complex catalyzes posttranscriptional tRNA modifications by attaching carboxy-methyl (cm 5 ) moieties to uridine bases located in the wobble position. The catalytic subunit Elp3 is highly conserved and harbors two individual subdomains, a radical S -adenosyl methionine (rSAM) and a lysine acetyltransferase (KAT) domain. The details of its modification reaction cycle and particularly the substrate specificity of its KAT domain remain elusive. Here, we present the co-crystal structure of bacterial Elp3 (DmcElp3) bound to an acetyl-CoA analog and compare it to the structure of a monomeric archaeal Elp3 from Methanocaldococcus infernus (MinElp3). Furthermore, we identify crucial active site residues, confirm the importance of the extended N-terminus for substrate recognition and uncover the specific induction of acetyl-CoA hydrolysis by different tRNA species. In summary, our results establish the clinically relevant Elongator subunit as a non-canonical acetyltransferase and genuine tRNA modification enzyme." @default.
- W2912786480 created "2019-02-21" @default.
- W2912786480 creator A5002261329 @default.
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- W2912786480 date "2019-02-07" @default.
- W2912786480 modified "2023-10-14" @default.
- W2912786480 title "The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase" @default.
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- W2912786480 doi "https://doi.org/10.1038/s41467-019-08579-2" @default.
- W2912786480 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6367351" @default.
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- W2912786480 hasPublicationYear "2019" @default.
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