Extremely Thermostable Elongation Factor G from Aquifex aeolicus: Cloning, Expression, Purification, and Characterization in a Heterologous Translation System
Author:
Publisher
Elsevier BV
Subject
Biotechnology
Reference25 articles.
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3. Three-dimensional structure of the ribosomal translocase: Elongation factor G from Thermus thermophilus;Avarsson;EMBO J.,1994
4. Crystal structure of active elongation factor Tu reveals major domain rearrangements;Berchtold;Nature,1993
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1. EF-G catalyzes tRNA translocation by disrupting interactions between decoding center and codon–anticodon duplex;Nature Structural & Molecular Biology;2014-08-10
2. Conformational transition of initiation factor 2 from the GTP- to GDP-bound state visualized on the ribosome;Nature Structural & Molecular Biology;2005-11-13
3. Structural Insights into Fusidic Acid Resistance and Sensitivity in EF-G;Journal of Molecular Biology;2005-05
4. Mutations in the G-domain of Elongation Factor G fromThermus thermophilus Affect Both Its Interaction with GTP and Fusidic Acid;Journal of Biological Chemistry;2001-08
5. Domain III of Elongation Factor G from Thermus thermophilus Is Essential for Induction of GTP Hydrolysis on the Ribosome;Journal of Biological Chemistry;2000-11
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