A molecular clamp ensures allosteric coordination of peptidyltransfer and ligand binding to the ribosomal A-site.

ABSTRACT: Although the ribosome is mainly comprised of rRNA and many of its critical functions occur through RNA-RNA interactions, distinct domains of ribosomal proteins also participate in switching the ribosome between different conformational/functional states. Prior studies demonstrated that two extended domains of ribosomal protein L3 form an allosteric switch between the pre- and post-translocational states. Missing was an explanation for how the movements of these domains are communicated among the ribosome's functional centers. Here, a third domain of L3 called the basic thumb, that protrudes roughly perpendicular from the W-finger and is nestled in the center of a cagelike structure formed by elements from three separate domains of the large subunit rRNA is investigated. Mutagenesis of basi

SUBMITTER: Meskauskas A 

PROVIDER: S-EPMC2995063 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature