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ABSTRACT:
SUBMITTER: Salsi E
PROVIDER: S-EPMC4297505 | biostudies-literature | 2015 Jan
REPOSITORIES: biostudies-literature
Salsi Enea E Farah Elie E Netter Zoe Z Dann Jillian J Ermolenko Dmitri N DN
Journal of molecular biology 20141115 2
Previous structural studies suggested that ribosomal translocation is accompanied by large interdomain rearrangements of elongation factor G (EF-G). Here, we follow the movement of domain IV of EF-G relative to domain II of EF-G using ensemble and single-molecule Förster resonance energy transfer. Our results indicate that ribosome-free EF-G predominantly adopts a compact conformation that can also, albeit infrequently, transition into a more extended conformation in which domain IV moves away f ...[more]