Reactivity of essential histidine residues in EF-Tu · GDP and EF-Tu · GTP from Escherichia coli
Author:
Publisher
Elsevier BV
Subject
Genetics,Biochemistry,Biophysics,Structural Biology
Reference21 articles.
1. The role of guanosine 5′-triphosphate in polypeptide chain elongation
2. A Model for the Tertiary Structure of p21, the Product of the ras Oncogene
3. Structure of the GDP Domain of EF-Tu and Location of the Amino Acids Homologous to ras Oncogene Proteins
4. Magnetic resonance studies of interactions of spin-labeled elongation factor Tu with ligands
5. Guanosine triphosphate and guanosine diphosphate as conformation-determining molecules. Differential interaction of a fluorescent probe with the guanosine nucleotide complexes of bacterial elongation factor Tu
Cited by 8 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. Interaction of EF-Tu with EF-Ts: substitution of His-118 in EF-Tu destabilizes the EF-Tu·EF-Ts complex but does not prevent EF-Ts from stimulating the release of EF-Tu-bound GDP;FEBS Letters;1998-01-30
2. Mapping Escherichia coli Elongation Factor Tu Residues Involved in Binding of Aminoacyl-tRNA;Journal of Biological Chemistry;1996-08
3. Histidine-118 of elongation factor Tu: its role in aminoacyl-tRNA binding and regulation of the GTPase activity;FEBS Letters;1994-04-18
4. Escherichia coli elongation-factor-Tu mutants with decreased affinity for aminoacyl-tRNA;European Journal of Biochemistry;1994-03
5. Topography of the Ternary EF-Tu/GTP/Phe-tRNAPhe Complex as Studied by Crosslinking and Limited Proteolysis;The Translational Apparatus;1993
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