2LCL

Solution Structure of RfaH carboxyterminal domain

Summary for 2LCL

• Entry DOI: 10.2210/pdb2lcl/pdb
• NMR Information: BMRB: 17615
• Descriptor: Transcriptional activator rfaH (1 entity in total)
• Functional Keywords: transcription, transcription pausing, transcription elongation, transcription antitermination
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 7269.33

Authors

Burmann, B.M.,Schweimer, K.,Roesch, P. (deposition date: 2011-05-02, release date: 2012-08-01, Last modification date: 2024-05-15)

Primary citation

Burmann, B.M.,Knauer, S.H.,Sevostyanova, A.,Schweimer, K.,Mooney, R.A.,Landick, R.,Artsimovitch, I.,Rosch, P.
An alpha helix to beta barrel domain switch transforms the transcription factor RfaH into a translation factor.
Cell(Cambridge,Mass.), 150:291-303, 2012

PubMed Abstract: NusG homologs regulate transcription and coupled processes in all living organisms. The Escherichia coli (E. coli) two-domain paralogs NusG and RfaH have conformationally identical N-terminal domains (NTDs) but dramatically different carboxy-terminal domains (CTDs), a β barrel in NusG and an α hairpin in RfaH. Both NTDs interact with elongating RNA polymerase (RNAP) to reduce pausing. In NusG, NTD and CTD are completely independent, and NusG-CTD interacts with termination factor Rho or ribosomal protein S10. In contrast, RfaH-CTD makes extensive contacts with RfaH-NTD to mask an RNAP-binding site therein. Upon RfaH interaction with its DNA target, the operon polarity suppressor (ops) DNA, RfaH-CTD is released, allowing RfaH-NTD to bind to RNAP. Here, we show that the released RfaH-CTD completely refolds from an all-α to an all-β conformation identical to that of NusG-CTD. As a consequence, RfaH-CTD binding to S10 is enabled and translation of RfaH-controlled operons is strongly potentiated. PAPERFLICK:

PubMed: 22817892
DOI: 10.1016/j.cell.2012.05.042

Experimental method

SOLUTION NMR