Mutation analysis of the functional role of amino acid residues in domain IV of elongation factor G
Author:
Publisher
Pleiades Publishing Ltd
Subject
Structural Biology,Biophysics
Link
http://link.springer.com/content/pdf/10.1134/S0026893306050116.pdf
Reference36 articles.
1. Spirin A.S. 2000. Ribosomes. N.Y.: Kluwer Academic/Plenum Publishers.
2. Czworkowski J., Wang J., Steitz T.A., Moore P.B. 1994. The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J. 13, 3661–3668.
3. Laurberg M., Kristensen O., Martemyanov K., Gudkov A.T., Nagaev I., Hughes D., Liljas A. 2000. Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. J. Mol. Biol. 303, 593–603.
4. Hansson S., Singh R., Gudkov A.T., Liljas A., Logan D.T. 2005. Crystal structure of a mutant elongation factor G trapped with a GTP analogue. FEBS Lett. 579, 4492–4497.
5. Moazed D., Robertson J.M., Noller H.F. 1988. Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23S RNA. Nature. 334, 362–364.
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. A Computational Study of Elongation Factor G (EFG) Duplicated Genes: Diverged Nature Underlying the Innovation on the Same Structural Template;PLoS ONE;2011-08-04
2. Amino acids Thr56 and Thr58 are not essential for elongation factor 2 function in yeast;FEBS Journal;2007-09-24
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