Ribosomal dynamics inferred from variations in experimental measurements.

ABSTRACT: The crystal structures of the ribosome reveal remarkable complexity and provide a starting set of snapshots with which to understand the dynamics of translation. To augment the static crystallographic models with dynamic information present in crosslink, footprint, and cleavage data, we examined 2691 proximity measurements and focused on the subset that was apparently incompatible with >40 published crystal structures. The measurements from this subset generally involve regions of the structure that are functionally conserved and structurally flexible. Local movements in the crystallographic states of the ribosome that would satisfy biochemical proximity measurements show coherent patterns suggesting alternative conformations of the ribosome. Three different types of data obtained for the

SUBMITTER: Gabashvili IS 

PROVIDER: S-EPMC1287051 | biostudies-literature | 2003 Nov

REPOSITORIES: biostudies-literature