| http://purl.uniprot.org/citations/25548166 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25548166 | http://www.w3.org/2000/01/rdf-schema#comment | "Many prokaryotes lack a tRNA synthetase to attach asparagine to its cognate tRNA(Asn), and instead synthesize asparagine from tRNA(Asn)-bound aspartate. This conversion involves two enzymes: a nondiscriminating aspartyl-tRNA synthetase (ND-AspRS) that forms Asp-tRNA(Asn), and a heterotrimeric amidotransferase GatCAB that amidates Asp-tRNA(Asn) to form Asn-tRNA(Asn) for use in protein synthesis. ND-AspRS, GatCAB, and tRNA(Asn) may assemble in an ∼400-kDa complex, known as the Asn-transamidosome, which couples the two steps of asparagine biosynthesis in space and time to yield Asn-tRNA(Asn). We report the 3.7-Å resolution crystal structure of the Pseudomonas aeruginosa Asn-transamidosome, which represents the most common machinery for asparagine biosynthesis in bacteria. We show that, in contrast to a previously described archaeal-type transamidosome, a bacteria-specific GAD domain of ND-AspRS provokes a principally new architecture of the complex. Both tRNA(Asn) molecules in the transamidosome simultaneously serve as substrates and scaffolds for the complex assembly. This architecture rationalizes an elevated dynamic and a greater turnover of ND-AspRS within bacterial-type transamidosomes, and possibly may explain a different evolutionary pathway of GatCAB in organisms with bacterial-type vs. archaeal-type Asn-transamidosomes. Importantly, because the two-step pathway for Asn-tRNA(Asn) formation evolutionarily preceded the direct attachment of Asn to tRNA(Asn), our structure also may reflect the mechanism by which asparagine was initially added to the genetic code."xsd:string |
| http://purl.uniprot.org/citations/25548166 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1423314112"xsd:string |
| http://purl.uniprot.org/citations/25548166 | http://purl.uniprot.org/core/author | "Kato K."xsd:string |
| http://purl.uniprot.org/citations/25548166 | http://purl.uniprot.org/core/author | "Nakamura A."xsd:string |
| http://purl.uniprot.org/citations/25548166 | http://purl.uniprot.org/core/author | "Suzuki T."xsd:string |
| http://purl.uniprot.org/citations/25548166 | http://purl.uniprot.org/core/author | "Soll D."xsd:string |
| http://purl.uniprot.org/citations/25548166 | http://purl.uniprot.org/core/author | "Tanaka I."xsd:string |
| http://purl.uniprot.org/citations/25548166 | http://purl.uniprot.org/core/author | "Yao M."xsd:string |
| http://purl.uniprot.org/citations/25548166 | http://purl.uniprot.org/core/author | "Sheppard K."xsd:string |
| http://purl.uniprot.org/citations/25548166 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25548166 | http://purl.uniprot.org/core/name | "Proc Natl Acad Sci U S A"xsd:string |
| http://purl.uniprot.org/citations/25548166 | http://purl.uniprot.org/core/pages | "382-387"xsd:string |
| http://purl.uniprot.org/citations/25548166 | http://purl.uniprot.org/core/title | "Structure of the Pseudomonas aeruginosa transamidosome reveals unique aspects of bacterial tRNA-dependent asparagine biosynthesis."xsd:string |
| http://purl.uniprot.org/citations/25548166 | http://purl.uniprot.org/core/volume | "112"xsd:string |
| http://purl.uniprot.org/citations/25548166 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/25548166 |
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