Structural highlights
Publication Abstract from PubMed
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.
Crystal structure of an Escherichia coli tRNA(Gly) microhelix at 2.0 A resolution.,Forster C, Brauer AB, Perbandt M, Lehmann D, Furste JP, Betzel Ch, Erdmann VA Biochem Biophys Res Commun. 2007 Nov 23;363(3):621-5. Epub 2007 Sep 14. PMID:17888869[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Forster C, Brauer AB, Perbandt M, Lehmann D, Furste JP, Betzel Ch, Erdmann VA. 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. Epub 2007 Sep 14. PMID:17888869 doi:http://dx.doi.org/10.1016/j.bbrc.2007.09.008
