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http://purl.uniprot.org/citations/30733442http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30733442http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30733442http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/30733442http://www.w3.org/2000/01/rdf-schema#comment"The Elongator complex catalyzes posttranscriptional tRNA modifications by attaching carboxy-methyl (cm5) 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."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.org/dc/terms/identifier"doi:10.1038/s41467-019-08579-2"xsd:string
http://purl.uniprot.org/citations/30733442http://purl.org/dc/terms/identifier"doi:10.1038/s41467-019-08579-2"xsd:string
http://purl.uniprot.org/citations/30733442http://purl.org/dc/terms/identifier"doi:10.1038/s41467-019-08579-2"xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/author"Lin T.Y."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/author"Lin T.Y."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/author"Abbassi N.E.H."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/author"Abbassi N.E.H."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/author"Chramiec-Glabik A."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/author"Chramiec-Glabik A."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/author"Glatt S."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/author"Glatt S."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/author"Jemiola-Rzeminska M."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/author"Jemiola-Rzeminska M."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/author"Rozycki J."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/author"Rozycki J."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/author"Zakrzewski K."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/author"Zakrzewski K."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/name"Nat. Commun."xsd:string
http://purl.uniprot.org/citations/30733442http://purl.uniprot.org/core/name"Nat. Commun."xsd:string