The crystal structure of unmodified tRNAPhe from Escherichia coli

被引：73

作者：

Byrne, Robert T. ^{[1
]}

Konevega, Andrey L. ^{[2
,3
]}

Rodnina, Marina V. ^{[2
]}

Antson, Alfred A. ^{[1
]}

机构：

[1] Univ York, Dept Chem, York Struct Biol Lab, Heslington YO10 5YW, N Yorkshire, England

[2] Max Planck Inst Biophys Chem, Dept Phys Biochem, D-37077 Gottingen, Germany

[3] Russian Acad Sci, Petersburg Nucl Phys Inst, Gatchina 188300, Russia

来源：

NUCLEIC ACIDS RESEARCH | 2010年 / 38卷 / 12期

基金：

英国生物技术与生命科学研究理事会; 英国惠康基金;

关键词：

PHENYLALANINE TRANSFER-RNA; ANTICODON STEM-LOOP; BINDING; CONFORMATION; TRNA(LYS; 3); STABILITY; DYNAMICS; TOOLS;

D O I：

10.1093/nar/gkq133

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Post-transcriptional nucleoside modifications fine-tune the biophysical and biochemical properties of transfer RNA (tRNA) so that it is optimized for participation in cellular processes. Here we report the crystal structure of unmodified tRNA(Phe) from Escherichia coli at a resolution of 3 angstrom. We show that in the absence of modifications the overall fold of the tRNA is essentially the same as that of mature tRNA. However, there are a number of significant structural differences, such as rearrangements in a triplet base pair and a widened angle between the acceptor and anticodon stems. Contrary to previous observations, the anticodon adopts the same conformation as seen in mature tRNA.

引用

页码：4154 / 4162

页数：9

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