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http://purl.uniprot.org/citations/16902403http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16902403http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16902403http://www.w3.org/2000/01/rdf-schema#comment"To ensure a high fidelity during translation, threonyl-tRNA synthetases (ThrRSs) harbor an editing domain that removes noncognate L-serine attached to tRNAThr. Most archaeal ThrRSs possess a unique editing domain structurally similar to D-aminoacyl-tRNA deacylases (DTDs) found in eubacteria and eukaryotes that specifically removes D-amino acids attached to tRNA. Here, we provide mechanistic insights into the removal of noncognate L-serine from tRNAThr by a DTD-like editing module from Pyrococcus abyssi ThrRS (Pab-NTD). High-resolution crystal structures of Pab-NTD with pre- and post-transfer substrate analogs and with L-serine show mutually nonoverlapping binding sites for the seryl moiety. Although the pre-transfer editing is excluded, the analysis reveals the importance of main chain atoms in proper positioning of the post-transfer substrate for its hydrolysis. A single residue has been shown to play a pivotal role in the inversion of enantioselectivity both in Pab-NTD and DTD. The study identifies an enantioselectivity checkpoint that filters opposite chiral molecules and thus provides a fascinating example of how nature has subtly engineered this domain for the selection of chiral molecules during translation."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7601278"xsd:string
http://purl.uniprot.org/citations/16902403http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7601278"xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Kruparani S.P."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Kruparani S.P."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Sankaranarayanan R."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Sankaranarayanan R."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Hussain T."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Hussain T."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Dock-Bregeon A.C."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Dock-Bregeon A.C."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Pal B."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Pal B."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Dwivedi S."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Dwivedi S."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Shekar M.R."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Shekar M.R."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Sureshbabu K."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/author"Sureshbabu K."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/16902403http://purl.uniprot.org/core/name"EMBO J."xsd:string