Literature DB >> 15922593

Elongation factors on the ribosome.

Jakob Nilsson1, Poul Nissen.   

Abstract

The ribosome is a complex macromolecular assembly capable of translating mRNA sequence into amino acid sequence. The adaptor molecule of translation is tRNA, but the delivery of aminoacyl-tRNAs--the primary substrate of the ribosome--relies on the formation of a ternary complex with elongation factor Tu (EF-Tu) and GTP. Likewise, elongation factor G (EF-G) is required to reset the elongation cycle through the translocation of tRNAs. Recent structures and biochemical data on ribosomes in complex with the ternary complex or EF-G have shed light on the mode of action of the elongation factors, and how this interplays with the state of tRNAs and the ribosome. A model emerges of the specific routes of conformational changes mediated by tRNA and the ribosome that trigger the GTPase activity of the elongation factors on the ribosome.

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Year:  2005        PMID: 15922593     DOI: 10.1016/j.sbi.2005.05.004

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  26 in total

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9.  Elongation factor 4 remodels the A-site tRNA on the ribosome.

Authors:  Matthieu G Gagnon; Jinzhong Lin; Thomas A Steitz
Journal:  Proc Natl Acad Sci U S A       Date:  2016-04-18       Impact factor: 11.205

10.  Triangle network motifs predict complexes by complementing high-error interactomes with structural information.

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