2P7V

Crystal structure of the Escherichia coli regulator of sigma 70, Rsd, in complex with sigma 70 domain 4

Summary for 2P7V

• Entry DOI: 10.2210/pdb2p7v/pdb
• Descriptor: Regulator of sigma D, RNA polymerase sigma factor rpoD, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: rsd, sigma 70, regulator of sigma 70, sigma 70 domain 4, transcription, regulation, helix-turn-helix, rsd-sigma 70 complex, sigma factor, escherichia coli rsd-sigma 70 complex, e. coli rsd-sigma 70 complex
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm (Potential): P0AFX4
• Total number of polymer chains: 2
• Total formula weight: 26268.31

Authors

Patikoglou, G.A.,Westblade, L.F.,Campbell, E.A.,Lamour, V.,Lane, W.J.,Darst, S.A. (deposition date: 2007-03-20, release date: 2007-08-21, Last modification date: 2024-02-21)

Primary citation

Patikoglou, G.A.,Westblade, L.F.,Campbell, E.A.,Lamour, V.,Lane, W.J.,Darst, S.A.
Crystal structure of the Escherichia coli regulator of sigma70, Rsd, in complex with sigma70 domain 4.
J.Mol.Biol., 372:649-659, 2007

PubMed Abstract: The Escherichia coli Rsd protein binds tightly and specifically to the RNA polymerase (RNAP) sigma(70) factor. Rsd plays a role in alternative sigma factor-dependent transcription by biasing the competition between sigma(70) and alternative sigma factors for the available core RNAP. Here, we determined the 2.6 A-resolution X-ray crystal structure of Rsd bound to sigma(70) domain 4 (sigma(70)(4)), the primary determinant for Rsd binding within sigma(70). The structure reveals that Rsd binding interferes with the two primary functions of sigma(70)(4), core RNAP binding and promoter -35 element binding. Interestingly, the most highly conserved Rsd residues form a network of interactions through the middle of the Rsd structure that connect the sigma(70)(4)-binding surface with three cavities exposed on distant surfaces of Rsd, suggesting functional coupling between sigma(70)(4) binding and other binding surfaces of Rsd, either for other proteins or for as yet unknown small molecule effectors. These results provide a structural basis for understanding the role of Rsd, as well as its ortholog, AlgQ, a positive regulator of Pseudomonas aeruginosa virulence, in transcription regulation.

PubMed: 17681541
DOI: 10.1016/j.jmb.2007.06.081

Experimental method

X-RAY DIFFRACTION (2.6 Å)