Crystal structure of the E. coli tRNA(Arg) aminoacyl stem isoacceptor RR-1660 at 2.0 A resolution

Autor:	André Eichert, Volker A. Erdmann, Jens P. Fürste, Markus Perbandt, Christian Betzel, Charlotte Förster, Dominik Oberthür, Angela Schreiber
Rok vydání:	2009
Předmět:	chemistry.chemical_classification Messenger RNA Biophysics RNA Context (language use) Aminoacylation RNA Transfer Arg Cell Biology Biology Genetic code Crystallography X-Ray Biochemistry Amino acid chemistry Helix Transfer RNA Escherichia coli Nucleic Acid Conformation Molecular Biology
Zdroj:	Biochemical and biophysical research communications. 385(1)
ISSN:	1090-2104
Popis:	Due to the redundancy of the genetic code there exist six mRNA codons for arginine and several tRNA(Arg) isoacceptors which translate these triplets to protein within the context of the mRNA. The tRNA identity elements assure the correct aminoacylation of the tRNA with the cognate amino acid by the aminoacyl-tRNA-synthetases. In tRNA(Arg), the identity elements consist of the anticodon, parts of the D-loop and the discriminator base. The minor groove of the acceptor stem interacts with the arginyl-tRNA-synthetase. We crystallized different Escherichia coli tRNA(Arg) acceptor stem helices and solved the structure of the tRNA(Arg) isoacceptor RR-1660 microhelix by X-ray structure analysis. The acceptor stem helix crystallizes in the space group P1 with the cell constants a=26.28, b=28.92, c=29.00 A, alpha=105.74, beta=99.01, gamma=97.44 degrees and two molecules per asymmetric unit. The RNA hydration pattern consists of 88 bound water molecules. Additionally, one glycerol molecule is bound within the interface of the two RNA molecules.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a17641696f85e13c9669964a20820723 https://pubmed.ncbi.nlm.nih.gov/19426710 Zobrazit plný text záznamu Full Text from ScienceDirect