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The 1.2 Å crystal structure of an E. coli tRNA acceptor stem microhelix reveals two magnesium binding sites |
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| Authors: | André Eichert,Angela Schreiber,Christian Betzel,Charlotte Fö rster |
| Affiliation: | a Institute of Chemistry and Biochemistry, Free University Berlin, Thielallee 63, 14195 Berlin, Germany b Institute of Biochemistry, Laboratory for Structural Biology of Infection and Inflammation, University of Lübeck, Building 22a, c/o DESY, 22603 Hamburg, Germany c Institute of Biochemistry and Food Chemistry, University of Hamburg, Notkestr. 85, Building 22a, c/o DESY, 22603 Hamburg, Germany |
| Abstract: | tRNA identity elements assure the correct aminoacylation of tRNAs by the cognate aminoacyl-tRNA synthetases. tRNASer belongs to the so-called class II system, in which the identity elements are rather simple and are mostly located in the acceptor stem region, in contrast to ‘class I’, where tRNA determinants are more complex and are located within different regions of the tRNA.The structure of an Escherichia coli tRNASer acceptor stem microhelix was solved by high resolution X-ray structure analysis. The RNA crystallizes in the space group C2, with one molecule per asymmetric unit and with the cell constants a = 35.79, b = 39.13, c = 31.37 Å, and β = 111.1°. A defined hydration pattern of 97 water molecules surrounds the tRNASer acceptor stem microhelix. Additionally, two magnesium binding sites were detected in the tRNASer aminoacyl stem. |
| Keywords: | tRNASer/Seryl-tRNA-synthetase tRNA acceptor stem microhelix X-ray structure Identity elements RNA hydration Magnesium binding sites |
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