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°.
|Journal||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|Number of pages||4|
|Publication status||Published - 13.02.2009|
Research Areas and Centers
- Academic Focus: Center for Infection and Inflammation Research (ZIEL)