Domain IV of elongation factor G fromThermus thermophilusis strictly required for translocation
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(99)00635-3/fullpdf
Reference37 articles.
1. The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution.
2. Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.
3. Crystal structure of active elongation factor Tu reveals major domain rearrangements
4. Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP Analog
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