Superposition of two tRNA{sup Ser} acceptor stem crystal structures: Comparison of structure, ligands and hydration
- Institute of Chemistry and Biochemistry, Free University Berlin, Thielallee 63, 14195 Berlin (Germany)
- Institute of Biochemistry and Molecular Biology, Laboratory for Structural Biology of Infection and Inflammation, University of Hamburg, c/o DESY, 22603 Hamburg (Germany)
We solved the X-ray structures of two Escherichia coli tRNA{sup Ser} acceptor stem microhelices. As both tRNAs are aminoacylated by the same seryl-tRNA-synthetase, we performed a comparative structure analysis of both duplexes to investigate the helical conformation, the hydration patterns and magnesium binding sites. It is well accepted, that the hydration of RNA plays an important role in RNA-protein interactions and that the extensive solvent content of the minor groove has a special function in RNA. The detailed comparison of both tRNA{sup Ser} microhelices provides insights into the structural arrangement of the isoacceptor tRNA aminoacyl stems with respect to the surrounding water molecules and may eventually help us to understand their biological function at atomic resolution.
- OSTI ID:
- 22202501
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 395, Issue 3; Other Information: Copyright (c) 2010 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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