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The zinc-binding site of Escherichia coli glutamyl-tRNA synthetase is located in the acceptor-binding domain. Studies by extended x-ray absorption fine structure, molecular modeling, and site-directed mutagenesis.
Liu J, Gagnon Y, Gauthier J, Furenlid L, L'Heureux PJ, Auger M, Nureki O, Yokoyama S, Lapointe J. Liu J, et al. Among authors: nureki o. J Biol Chem. 1995 Jun 23;270(25):15162-9. doi: 10.1074/jbc.270.25.15162. J Biol Chem. 1995. PMID: 7797500 Free article.
[Aminoacyl-tRNA synthetase].
Nureki O, Yokoyama S. Nureki O, et al. Tanpakushitsu Kakusan Koso. 1994 May;39(7):1215-25. Tanpakushitsu Kakusan Koso. 1994. PMID: 8016351 Review. Japanese. No abstract available.
Chemical modification and mutagenesis studies on zinc binding of aminoacyl-tRNA synthetases.
Nureki O, Kohno T, Sakamoto K, Miyazawa T, Yokoyama S. Nureki O, et al. J Biol Chem. 1993 Jul 25;268(21):15368-73. J Biol Chem. 1993. PMID: 8340367 Free article.
Thermus thermophilus methionyl-tRNA synthetase consists of two identical subunits with a potential Zn(2+)-binding sequence of Cys-X2-Cys-X13-Cys-X2-His (Nureki, O., Muramatsu, T., Suzuki, K., Kohda, D., Matsuzawa, H., Ohta, T. Miyazawa, T., and Yokoyama, S. (1991) J …
Thermus thermophilus methionyl-tRNA synthetase consists of two identical subunits with a potential Zn(2+)-binding sequence of Cys-X2-Cys-X13 …
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