Crystal structure of an Escherichia coli tRNA(Gly) microhelix at 2.0 A resolution

C Förster; A B E Brauer; M Perbandt; D Lehmann; J P Fürste; Ch Betzel; V A Erdmann

doi:10.1016/j.bbrc.2007.09.008

Crystal structure of an Escherichia coli tRNA(Gly) microhelix at 2.0 A resolution

Biochem Biophys Res Commun. 2007 Nov 23;363(3):621-5. doi: 10.1016/j.bbrc.2007.09.008. Epub 2007 Sep 14.

Authors

C Förster¹, A B E Brauer, M Perbandt, D Lehmann, J P Fürste, Ch Betzel, V A Erdmann

Affiliation

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

PMID: 17888869
DOI: 10.1016/j.bbrc.2007.09.008

Abstract

tRNA identity elements determine the correct aminoacylation by the cognate aminoacyl-tRNA synthetase. In class II aminoacyl tRNA synthetase systems, tRNA specificity is assured by rather few and simple recognition elements, mostly located in the acceptor stem of the tRNA. Here we present the crystal structure of an Escherichia coli tRNA(Gly) aminoacyl stem microhelix at 2.0 A resolution. The tRNA(Gly) microhelix crystallizes in the space group P3(2)21 with the cell constants a=b=35.35 A, c=130.82 A, gamma=120 degrees . The helical parameters, solvent molecules and a potential magnesium binding site are discussed.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Base Sequence
Crystallization
Escherichia coli / genetics*
Models, Molecular
Nucleic Acid Conformation*
RNA, Transfer, Gly / chemistry*
RNA, Transfer, Gly / genetics
X-Ray Diffraction

Substances

RNA, Transfer, Gly