Two-step pathway to aminoacylated tRNA.
The 3.0 Angstrom crystal structure of a tRNA-dependent amidotransferase from the hyperthermophilic archaeon Pyrococcus abyssi provides the first detailed insight into how cells lacking canonical tRNA synthetases nonetheless carry out protein synthesis with high fidelity.
Perona
John J
JJ
Department of Chemistry and Biochemistry, University of California, Santa Barbara, Santa Barbara, California 93106, USA.
D000244:Adenosine Diphosphate / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D005975:Glutamate-tRNA Ligase / Q000378:metabolism; D019884:Nitrogenous Group Transferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D014176:Protein Biosynthesis; D043903:Pyrococcus abyssi / Q000201:enzymology; D019642:RNA, Archaeal / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D012329:RNA, Bacterial / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012343:RNA, Transfer / Q000737:chemistry* / Q000378:metabolism*; D012351:RNA, Transfer, Gln / Q000378:metabolism
D019642:RNA, Archaeal; D012329:RNA, Bacterial; D012351:RNA, Transfer, Gln; D000244:Adenosine Diphosphate; D012343:RNA, Transfer; D019884:Nitrogenous Group Transferases; D005975:Glutamate-tRNA Ligase