Literature DB >> 17888869

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

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

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.

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Year:  2007        PMID: 17888869     DOI: 10.1016/j.bbrc.2007.09.008

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  1 in total

1.  X-ray diffraction analysis of a human tRNA(Gly) acceptor-stem microhelix isoacceptor at 1.18 A resolution.

Authors:  André Eichert; Markus Perbandt; Angela Schreiber; Jens P Fürste; Christian Betzel; Volker A Erdmann; Charlotte Förster
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2008-12-25
  1 in total

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