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Crystal structure of the Tyrosyl-tRNA synthetase (TyrRS) in Nanoarchaeum equitansCrystal structure of the Tyrosyl-tRNA synthetase (TyrRS) in Nanoarchaeum equitans
Structural highlights
FunctionSYY_NANEQ Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).[HAMAP-Rule:MF_02009] Publication Abstract from PubMedtRNA(Tyr) of Nanoarchaeum equitans has a remarkable feature with an extra guanosine residue at the 5'-terminus. However, the N. equitans tRNA(Tyr) mutant without extra guanosine at the 5'-end was tyrosylated by tyrosyl-tRNA synthase (TyrRS). We solved the crystal structure of N. equitans TyrRS at 2.80 A resolution. By comparing the present solved structure with the complex structures TyrRS with tRNA(Tyr) of Thermus thermophilus and Methanocaldococcus jannaschii, an arginine substitution mutant of N. equitans TyrRS at Ile200 (I200R), which is the putative closest candidate to the 5'-phosphate of C1 of N. equitans tRNA(Tyr), was prepared. The I200R mutant tyrosylated not only wild-type tRNA(Tyr) but also the tRNA without the G-1 residue. Further tyrosylation analysis revealed that the second base of the anticodon (U35), discriminator base (A73), and C1:G72 base pair are strong recognition sites. Crystal structure of Nanoarchaeum equitans tyrosyl-tRNA synthetase and its aminoacylation activity toward tRNA(Tyr) with an extra guanosine residue at the 5'-terminus.,Horikoshi T, Noguchi H, Umehara T, Mutsuro-Aoki H, Kurihara R, Noguchi R, Hashimoto T, Watanabe Y, Ando T, Kamata K, Park SY, Tamura K Biochem Biophys Res Commun. 2021 Aug 27;575:90-95. doi:, 10.1016/j.bbrc.2021.08.070. PMID:34461441[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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