Crystallographic structures of ribosomal proteins and elongation factor G
نویسندگان
چکیده
منابع مشابه
Identity of the ribosomal proteins involved in the interaction with elongation factor G.
Rabbit antibodies produced against 50 of the 55 individually purified ribosomal proteins of Escherichia coli were tested for their ability to interfere with the formation of the ribosome.EF-G.GDP complex. Only antibodies produced against proteins L7 and L12 inhibited complex formation, and they did so completely. These two proteins were previously shown to be immunologically indistinguishable a...
متن کاملAllosteric collaboration between elongation factor G and the ribosomal L1 stalk directs tRNA movements during translation.
Determining the mechanism by which tRNAs rapidly and precisely transit through the ribosomal A, P, and E sites during translation remains a major goal in the study of protein synthesis. Here, we report the real-time dynamics of the L1 stalk, a structural element of the large ribosomal subunit that is implicated in directing tRNA movements during translation. Within pretranslocation ribosomal co...
متن کاملFollowing movement of domain IV of elongation factor G during ribosomal translocation.
Translocation of mRNA and tRNAs through the ribosome is catalyzed by a universally conserved elongation factor (EF-G in prokaryotes and EF-2 in eukaryotes). Previous studies have suggested that ribosome-bound EF-G undergoes significant structural rearrangements. Here, we follow the movement of domain IV of EF-G, which is critical for the catalysis of translocation, relative to protein S12 of th...
متن کاملStimulation of the GTPase activity of translation elongation factor G by ribosomal protein L7/12.
Elongation factors (EFs) Tu and G are GTPases that have important functions in protein synthesis. The low intrinsic GTPase activity of both factors is strongly stimulated on the ribosome by unknown mechanisms. Here we report that isolated ribosomal protein L7/12 strongly stimulates GTP hydrolysis by EF-G, but not by EF-Tu, indicating a major contribution of L7/12 to GTPase activation of EF-G on...
متن کاملControl of phosphate release from elongation factor G by ribosomal protein L7/12.
Ribosomal protein L7/12 is crucial for the function of elongation factor G (EF-G) on the ribosome. Here, we report the localization of a site in the C-terminal domain (CTD) of L7/12 that is critical for the interaction with EF-G. Single conserved surface amino acids were replaced in the CTD of L7/12. Whereas mutations in helices 5 and 6 had no effect, replacements of V66, I69, K70, and R73 in h...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 1996
ISSN: 0108-7673
DOI: 10.1107/s0108767396092677