Interdomain Contacts Control Native State Switching of RfaH on a Dual-Funneled Landscape.

ABSTRACT: RfaH is a virulence factor from Escherichia coli whose C-terminal domain (CTD) undergoes a dramatic α-to-β conformational transformation. The CTD in its α-helical fold is stabilized by interactions with the N-terminal domain (NTD), masking an RNA polymerase binding site until a specific recruitment site is encountered. Domain dissociation is triggered upon binding to DNA, allowing the NTD to interact with RNA polymerase to facilitate transcription while the CTD refolds into the β-barrel conformation that interacts with the ribosome to activate translation. However, structural details of this transformation process in the context of the full protein remain to be elucidated. Here, we explore the mechanism of the α-to-β conformational transition of RfaH in the full-length protein using a dual

SUBMITTER: Ramirez-Sarmiento CA 

PROVIDER: S-EPMC4521827 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature