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Publication Abstract from PubMed

This study reports the X-ray crystallographic structure of the glycyl-tRNA synthetase (GlyRS) of Nanoarchaeum equitans - a hyperthermophilic archaeal species. This is the first archaeal GlyRS crystal structure elucidated. The GlyRS comprises an N-terminal catalytic domain and a C-terminal anticodon-binding domain with a long beta-sheet inserted between these domains. An unmodified transcript of the wild-type N. equitans tRNA(Gly) was successfully glycylated using GlyRS. Substitution of the discriminator base A73 of tRNA(Gly) with any other nucleotide caused a significant decrease in glycylation activity. Mutational analysis of the second base-pair C2G71 of the acceptor stem of tRNA(Gly) elucidated the importance of the base-pair, especially G71, as an identity element for recognition by GlyRS. Glycylation assays using tRNA(Gly) G71 substitution mutants and a GlyRS mutant where Arg223 is mutated to alanine strengthen the possibility that the carbonyl oxygen at position 6 of G71 would hydrogen-bond with the guanidine nitrogen of Arg223 in N. equitans GlyRS.

Glycyl-tRNA synthetase from Nanoarchaeum equitans: The first crystal structure of archaeal GlyRS and analysis of its tRNA glycylation.,Fujisawa A, Toki R, Miyake H, Shoji T, Doi H, Hayashi H, Hanabusa R, Mutsuro-Aoki H, Umehara T, Ando T, Noguchi H, Voet A, Park SY, Tamura K Biochem Biophys Res Commun. 2019 Apr 2;511(2):228-233. doi:, 10.1016/j.bbrc.2019.01.142. Epub 2019 Feb 13. PMID:30771900^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.