| Literature DB >> 10371036 |
M V Rodnina1, A Savelsbergh, W Wintermeyer.
Abstract
The translocation step of protein elongation entails a large-scale rearrangement of the tRNA-mRNA-ribosome complex. Recent years have seen major advances in unraveling the mechanism of the process on the molecular level. A number of intermediate states have been defined and, in part, characterized structurally. The article reviews the recent evidence that suggests a dynamic role of the ribosome and its ligands during translocation. The focus is on dynamic aspects of tRNA movement and on the role of elongation factor G and GTP hydrolysis in translocation catalysis. The significance of structural changes of the ribosome induced by elongation factor G as well the role of ribosomal RNA are addressed. A functional model of elongation factor G as a motor protein driven by GTP hydrolysis is discussed.Entities:
Mesh：
Substances：
Year: 1999 PMID： 10371036 DOI： 10.1111/j.1574-6976.1999.tb00402.x
Source DB: PubMed Journal: FEMS Microbiol Rev ISSN： 0168-6445 Impact factor: 16.408