Movement of Elongation Factor G between Compact and Extended Conformations
نویسندگان
چکیده
منابع مشابه
Large-Scale Movement of Elongation Factor G and Extensive Conformational Change of the Ribosome during Translocation
Elongation factor (EF) G promotes tRNA translocation on the ribosome. We present three-dimensional reconstructions, obtained by cryo-electron microscopy, of EF-G-ribosome complexes before and after translocation. In the pretranslocation state, domain 1 of EF-G interacts with the L7/12 stalk on the 50S subunit, while domain 4 contacts the shoulder of the 30S subunit in the region where protein S...
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 کاملBrownian dynamics study of the association between the 70S ribosome and elongation factor G
Protein synthesis on the ribosome involves a number of external protein factors that bind at its functional sites. One key factor is the elongation factor G (EF-G) that facilitates the translocation of transfer RNAs between their binding sites, as well as advancement of the messenger RNA by one codon. The details of the EF-G/ribosome diffusional encounter and EF-G association pathway still rema...
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 کاملStructural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations.
The highly conserved ClpP protease consists of two heptameric rings that interact by the interdigitation of an alpha-helix beta strand handle domain motif to form a tetradecameric cylinder. We previously proposed that protease dynamics results in the temporary unstructuring of interacting pairs of handle domains, opening transient equatorial side pores that allow for peptide egress. Here, we re...
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ژورنال
عنوان ژورنال: Journal of Molecular Biology
سال: 2015
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2014.11.010