Superposition of two tRNASer acceptor stem crystal structures: comparison of structure, ligands and hydration
| Autor: | Christian Betzel, André Eichert, Volker A. Erdmann, Jens P. Fürste, Alexander K.C. Ulrich, Charlotte Förster |
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| Rok vydání: | 2010 |
| Předmět: |
Binding Sites
Magnesium binding Base Sequence Chemistry Stereochemistry Biophysics RNA Cell Biology Crystal structure Crystallography X-Ray Biochemistry Acceptor Crystallography Atomic resolution Transfer RNA Escherichia coli Molecule Nucleic Acid Conformation Magnesium Molecular Biology Function (biology) RNA Transfer Ser |
| Zdroj: | Biochemical and biophysical research communications. 395(3) |
| ISSN: | 1090-2104 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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