Escherichia coli tRNAArg acceptor-stem isoacceptors: Comparative crystallization and preliminary X-ray diffraction analysis

André Eichert, Angela Schreiber, Jens P. Fürste, Markus Perbandt, Christian Betzel, Volker A. Erdmann, Charlotte Förster*

*Corresponding author for this work
1 Citation (Scopus)

Abstract

The aminoacylation of tRNA is a crucial step in cellular protein biosynthesis. Recognition of the cognate tRNA by the correct aminoacyl-tRNA synthetase is ensured by tRNA identity elements. In tRNAArg, the identity elements consist of the anticodon, parts of the D-loop and the discriminator base. The minor groove of the aminoacyl stem interacts with the arginyl-tRNA synthetase. As a consequence of the redundancy of the genetic code, six tRNAArg isoacceptors exist. In the present work, three different Escherichia coli tRNAArg acceptor-stem helices were crystallized. Two of them, the tRNAArg microhelices RR-1660 and RR-1662, were examined by X-ray diffraction analysis and diffracted to 1.7 and 1.8 Å resolution, respectively. The tRNAArg RR-1660 helix crystallized in space group P1, with unit-cell parameters a = 26.28, b = 28.92, c = 29.00 Å, α = 105.74, β = 99.01, γ = 97.44°, whereas the tRNAArg RR-1662 helix crystallized in space group C2, with unit-cell parameters a = 33.18, b = 46.16, c = 26.04 Å, β = 101.50°.

Original languageEnglish
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number2
Pages (from-to)98-101
Number of pages4
ISSN1744-3091
DOIs
Publication statusPublished - 13.02.2009

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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