2LCL: Solution Structure of RfaH carboxyterminal domain

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 beta barrel in NusG and an alpha 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-alpha to an all-beta 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:
PDB ID: 2LCLDownload
MMDB ID: 101553
PDB Deposition Date: 2011/5/2
Updated in MMDB: 2012/08
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2LCL: monomeric; determined by author
Molecular Components in 2LCL
Label Count Molecule
Protein (1 molecule)
Transcriptional Activator Rfah(Gene symbol: rfaH)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB