caa a22 4500 463185854 CHVBK 20180406164852.0 cr unu---uuuuu 170326e20070501xx s 000 0 eng 10.1007/s00726-006-0436-5 doi (NATIONALLICENCE)springer-10.1007/s00726-006-0436-5 Crystallization and preliminary X-ray diffraction analysis of E. coli arginyl-tRNA synthetase in complex form with a tRNAArg [Elektronische Daten] [M. Zhou, A. Azzi, X. Xia, E.-D. Wang, S.-X. Lin] Summary.: Amino acids are building blocks of proteins, while aminoacyl-tRNA synthetases (aaRSs) catalyze the first reaction in such building: the biosynthesis of proteins. The E. coli arginyl-tRNA synthetase (ArgRS) has been crystallized in complex form with tRNAArg (B. stearothermophilus), at pH 5.6 using ammonium sulfate as a precipitating agent. Two crystal forms have been identified based on unit cell dimension. The complete data sets from both crystal forms have been collected with a primitive hexagonal space group. A data set of Form II crystals at 3.2 Å and 94% completeness has been obtained, with unit cell parameters a = b = 98.0 Å, c = 463.2 Å, and α = β = 90°, γ = 120°, being different from a = b = 110.8 Å, c = 377.8 Å for form I. The structure determination will demonstrate the interaction of these two macromolecules to understand the special mechanism of ArgRS that requires the presence of tRNA for amino acid activation. Such complex structure also provides a wide opening for inhibitor search using bioinformatics. Springer-Verlag, 2006 Keywords: Amino acids - Arginyl-tRNA synthetase - tRNAArg - Protein-RNA complex - Macromolecular crystallization - Amino acid activation - Aminoacylation - Protein biosynthesis nationallicence Zhou M. Laboratory of Molecular Endocrinology, CHUL Research Center and Laval University, Québec, Canada aut Azzi A. Laboratory of Molecular Endocrinology, CHUL Research Center and Laval University, Québec, Canada aut Xia X. State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology (SIBCB), Shanghai Institutes of Biological Sciences (SIBS), Shanghai, China aut Wang E.-D State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology (SIBCB), Shanghai Institutes of Biological Sciences (SIBS), Shanghai, China aut Lin S.-X Laboratory of Molecular Endocrinology, CHUL Research Center and Laval University, Québec, Canada aut Amino Acids Springer-Verlag 32/4(2007-05-01), 479-482 0939-4451 32:4<479 2007 32 726 https://doi.org/10.1007/s00726-006-0436-5 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00726-006-0436-5 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Zhou M. Laboratory of Molecular Endocrinology, CHUL Research Center and Laval University, Québec, Canada aut NATIONALLICENCE 700 1- Azzi A. Laboratory of Molecular Endocrinology, CHUL Research Center and Laval University, Québec, Canada aut NATIONALLICENCE 700 1- Xia X. State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology (SIBCB), Shanghai Institutes of Biological Sciences (SIBS), Shanghai, China aut NATIONALLICENCE 700 1- Wang E.-D State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology (SIBCB), Shanghai Institutes of Biological Sciences (SIBS), Shanghai, China aut NATIONALLICENCE 700 1- Lin S.-X Laboratory of Molecular Endocrinology, CHUL Research Center and Laval University, Québec, Canada aut NATIONALLICENCE 773 0- Amino Acids Springer-Verlag 32/4(2007-05-01), 479-482 0939-4451 32:4<479 2007 32 726 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer