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Crystal structure of the human tRNAGly microhelix isoacceptor G9990 at 1.18A resolution

DOI: 10.1016/j.bbrc.2009.01.127 DOI Help
PMID: 19284994 PMID Help

Authors: A. Eichert (Institute of Chemistry and Biochemistry, Free University Berlin) , M. Perbandt (Institute of Chemistry and Biochemistry, Free University Berlin) , A. Schreiber (Institute of Chemistry and Biochemistry, Free University Berlin) , J. P. Fürste (Institute of Chemistry and Biochemistry, Free University Berlin) , C. Betzel (Institute of Chemistry and Biochemistry, Free University Berlin) , V. A. Erdmann (Institute of Chemistry and Biochemistry, Free University Berlin) , C. Förster (Institute of Chemistry and Biochemistry, Free University Berlin)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Biochemical And Biophysical Research Communications , VOL 380 , PAGES 503 - 507

State: Published (Approved)
Published: January 2009

Abstract: The tRNAGly/Glycyl-tRNA synthetase system belongs to the so called ‘class II’ in which tRNA identity elements consist of relative few and simple motifs, as compared to ‘class I’ where the tRNA determinants are more complicated and spread over different parts of the tRNA, mostly including the anticodon. The determinants from ‘class II’ although, are located in the aminoacyl stem and sometimes include the discriminator base. There exist predominant structure differences for the Glycyl-tRNA-synthetases and for the tRNAGly identity elements comparing eucaryotic/archaebacterial and eubacterial systems. We focus on comparative X-ray structure analysis of tRNAGly acceptor stem microhelices from different organisms. Here, we report the X-ray structure of the human tRNAGly microhelix isoacceptor G9990 at 1.18 Å resolution. Superposition experiments to another human tRNAGly microhelix and a detailed comparison of the RNA hydration patterns show a great number of water molecules with identical positions in both RNAs. This is the first structure comparison of hydration layers from two isoacceptor tRNA microhelices with a naturally occurring base pair exchange.

Journal Keywords: tRNA identity elements; Acceptor stem microhelix; Glycyl-tRNA-synthetase/tRNAGly system; Crystal structure; RNA hydration pattern; Superposition experiments; Comparative structure analysis

Subject Areas: Biology and Bio-materials


Instruments: I04-Macromolecular Crystallography

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