E. coli elongation factor Tu bound to a GTP analogue displays an open conformation equivalent to the GDP-bound form
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چکیده
منابع مشابه
The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation.
BACKGROUND Elongation factor Tu (EF-Tu) is a GTP-binding protein that is crucial for protein biosynthesis. In the GTP form of the molecule, EF-Tu binds tightly to aminoacyl-tRNA, forming a ternary complex that interacts with the ribosomal acceptor site. During this interaction, GTP is hydrolyzed, and EF-Tu.GDP is ejected. RESULTS The crystal structure of EF-Tu from Thermus aquaticus, complexe...
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Kirromycin, also known as mccimycin, is a member of the elfamycin family of antibiotics. These antibiotics inhibit bacterial protein synthesis by binding tightly to elongation factor Tu (Emu) a 43.2 kD G-protein. E m u .GTP is able to carry aminoacyl tRNA to the ribosome in the presence of kirromycin in the usual way, but after hydrolysis of GTP EFTu.GDP is unable to leave the ribosome. Consequ...
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Translation initiation factor 2 (IF2) is involved in the early steps of bacterial protein synthesis. It promotes the stabilization of the initiator tRNA on the 30S initiation complex (IC) and triggers GTP hydrolysis upon ribosomal subunit joining. While the structure of an archaeal homologue (a/eIF5B) is known, there are significant sequence and functional differences in eubacterial IF2, while ...
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For any transferable utility game in coalitional form with a nonempty core, we show that that the number of blocks required to switch from an imputation out of the core to an imputation in the core is at most n−1, where n is the number of players. This bound exploits the geometry of the core and is optimal. It considerably improves the upper bounds found so far by Kóczy [7], Yang [13, 14] and a...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 2018
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/gky697