Histidine-118 of elongation factor Tu: its role in aminoacyl-tRNA binding and regulation of the GTPase activity
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(94)80614-4/fullpdf
Reference30 articles.
1. Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography.
2. Structure of the GDP Domain of EF-Tu and Location of the Amino Acids Homologous to ras Oncogene Proteins
3. Refined structure of elongation factor EF-Tu from Escherichia coli
4. Crystal structure of active elongation factor Tu reveals major domain rearrangements
5. The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
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1. Bacterial elongation factors EF-Tu, their mutants, chimeric forms, and domains: Isolation and purification;Journal of Chromatography B;2007-04
2. Directed Mutagenesis Identifies Amino Acid Residues Involved in Elongation Factor Tu Binding to yeast Phe-tRNAPhe;Journal of Molecular Biology;2007-04
3. The Importance of P-loop and Domain Movements in EF-Tu for Guanine Nucleotide Exchange;Journal of Biological Chemistry;2006-07
4. Opposite roles of domains 2+3 of Escherichia coli EF-Tu and Bacillus stearothermophilus EF-Tu in the regulation of EF-Tu GTPase activity;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2005-08
5. Nucleotide-dependent Binding of the GTPase Domain of the Signal Recognition Particle Receptor β-Subunit to the α-Subunit;Journal of Biological Chemistry;2000-09
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