Escherichia coli tRNAArg acceptor‐stem isoacceptors: comparative crystallization and preliminary X‐ray diffraction analysis
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°.
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