转移RNA
鸟嘌呤
蛋白质亚单位
生物
生物化学
核糖核酸
核苷酸
基因
作者
Katharina Sievers,Piotr Neumann,Lukas Sušac,Stefano Da Vela,Melissa A. Graewert,Simon Trowitzsch,Dmitri I. Svergun,Robert Tampé,Ralf Ficner
出处
期刊:Structure
[Elsevier]
日期:2024-03-01
卷期号:32 (3): 316-327.e5
被引量:1
标识
DOI:10.1016/j.str.2023.12.006
摘要
Eukaryotic tRNA guanine transglycosylase (TGT) is an RNA-modifying enzyme which catalyzes the base exchange of the genetically encoded guanine 34 of tRNAsAsp,Asn,His,Tyr for queuine, a hypermodified 7-deazaguanine derivative. Eukaryotic TGT is a heterodimer comprised of a catalytic and a non-catalytic subunit. While binding of the tRNA anticodon loop to the active site is structurally well understood, the contribution of the non-catalytic subunit to tRNA binding remained enigmatic, as no complex structure with a complete tRNA was available. Here, we report a cryo-EM structure of eukaryotic TGT in complex with a complete tRNA, revealing the crucial role of the non-catalytic subunit in tRNA binding. We decipher the functional significance of these additional tRNA-binding sites, analyze solution state conformation, flexibility, and disorder of apo TGT, and examine conformational transitions upon tRNA binding.
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