ArticleActa crystallographica. Section F, Structural biology communications2014
Crystallization and preliminary X-ray crystallographic analysis of a bacterial Asn-transamidosome.
Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed, 4 citations in OpenAlex.
- Crystal structures reveal an elusive functional domain of pyrrolysyl-tRNA synthetase.Nature chemical biology · 2017Article
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5 authors at 1 institution in 1 country.
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Abstract
Most canonical aminoacyl-tRNAs are synthesized directly by their cognate aminoacyl-tRNA synthetases (aaRSs), but glutaminyl-tRNA(Gln) and asparaginyl-tRNA(Asn) are synthesized indirectly by two-step processes. These processes are catalyzed by the transamidosome, a large ribonucleoprotein particle composed of GatA, GatB, GatC, aaRS and tRNA. In this study, the Asn-transamidosome from Pseudomonas aeruginosa was reconstructed and crystallized by mixing purified GatCAB complex, AspRS and tRNA(Asn). The crystal of the Asn-transamidosome belonged to space group P2₁, with unit-cell parameters a=93.3, b=186.0, c=287.8 Å, β=93.3°, and diffracted to 3.73 Å resolution. Preliminary X-ray crystallographic analysis showed that the asymmetric unit contained two Asn-transamidosomes, each composed of two GatCABs, one AspRS dimer and two tRNAAsns, indicating that the construction of the current Asn-transamidosome differs from that of Thermus thermophilus.
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