Form follows function: Structure of an elongation factor G-ribosome complex
نویسندگان
چکیده
منابع مشابه
Form follows function: structure of an elongation factor G-ribosome complex.
Not so long ago, the idea of deriving functional models from just looking at large subcellular structures in different functional states seemed unrealistic. In the meantime, the visualization of such structures by three-dimensional reconstructions from cryoelectron microscopic images has made enormous progress. Studies on ribosomes, from both prokaryotes and eukaryotes, have been particularly r...
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Thiostrepton, a macrocyclic thiopeptide antibiotic, inhibits prokaryotic translation by interfering with the function of elongation factor G (EF-G). Here, we have used 70S ribosome binding and GTP hydrolysis assays to study the effects of thiostrepton on EF-G and a newly described translation factor, elongation factor 4 (EF4). In the presence of thiostrepton, ribosome-dependent GTP hydrolysis i...
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Emotion research has been divided by debate as to whether emotions are universal in form or cognitively constructed. We review an emerging approach that focuses on function rather than form. Functional affective science suggests that the particular origin of an emotion is relatively unimportant; instead, emotions can be understood in terms of a rapidly deployed set of mechanisms that structure ...
متن کاملThe structure of the ribosome with elongation factor G trapped in the posttranslocational state.
Elongation factor G (EF-G) is a guanosine triphosphatase (GTPase) that plays a crucial role in the translocation of transfer RNAs (tRNAs) and messenger RNA (mRNA) during translation by the ribosome. We report a crystal structure refined to 3.6 angstrom resolution of the ribosome trapped with EF-G in the posttranslocational state using the antibiotic fusidic acid. Fusidic acid traps EF-G in a co...
متن کاملStructure of the ribosome with elongation factor G trapped in the pretranslocation state.
During protein synthesis, tRNAs and their associated mRNA codons move sequentially on the ribosome from the A (aminoacyl) site to the P (peptidyl) site to the E (exit) site in a process catalyzed by a universally conserved ribosome-dependent GTPase [elongation factor G (EF-G) in prokaryotes and elongation factor 2 (EF-2) in eukaryotes]. Although the high-resolution structure of EF-G bound to th...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1998
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.95.13.7237