Intrinsic dynamics of the partly unstructured PX domain from the Sendai virus RNA polymerase cofactor P.

ABSTRACT: Despite their evident importance for function, dynamics of intrinsically unstructured proteins are poorly understood. Sendai virus phosphoprotein, cofactor of the RNA polymerase, contains a partly unstructured protein domain. The phosphoprotein X domain (PX) is responsible for binding the polymerase to the nucleocapsid assembling the viral RNA. For RNA synthesis, the interplay of the dynamics of the unstructured and structured PX subdomains is thought to drive progression of the RNA polymerase along the nucleocapsid. Here we present a detailed study of the dynamics of PX using hydrogen/deuterium exchange and different NMR relaxation measurements. In the unstructured subdomain, large amplitude fast motions were found to be fine-tuned by the presence of residues with short side chains. In th

SUBMITTER: Houben K 

PROVIDER: S-EPMC1989709 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature