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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Feb 1;65(Pt 2):98-101. doi: 10.1107/S1744309108042012. Epub 2009 Jan 7.

Escherichia coli tRNA(Arg) acceptor-stem isoacceptors: comparative crystallization and preliminary X-ray diffraction analysis.

Author information

1
Institute of Chemistry and Biochemistry, Free University Berlin, Thielallee 63, 14195 Berlin, Germany.

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 tRNA(Arg), 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 tRNA(Arg) isoacceptors exist. In the present work, three different Escherichia coli tRNA(Arg) acceptor-stem helices were crystallized. Two of them, the tRNA(Arg) microhelices RR-1660 and RR-1662, were examined by X-ray diffraction analysis and diffracted to 1.7 and 1.8 A resolution, respectively. The tRNA(Arg) RR-1660 helix crystallized in space group P1, with unit-cell parameters a = 26.28, b = 28.92, c = 29.00 A, alpha = 105.74, beta = 99.01, gamma = 97.44 degrees , whereas the tRNA(Arg) RR-1662 helix crystallized in space group C2, with unit-cell parameters a = 33.18, b = 46.16, c = 26.04 A, beta = 101.50 degrees .

PMID:
19193994
PMCID:
PMC2635860
DOI:
10.1107/S1744309108042012
[Indexed for MEDLINE]
Free PMC Article

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