2MZ8

Solution NMR structure of Salmonella Typhimurium transcriptional regulator protein Crl

Summary for 2MZ8

• Entry DOI: 10.2210/pdb2mz8/pdb
• NMR Information: BMRB: 25476
• Descriptor: Sigma factor-binding protein Crl (1 entity in total)
• Functional Keywords: crl, salmonella enterica, serovar typhimurium, sigmas, sigma factor binding protein, sigma factor activator, stationary phase, stress response, transcriptional regulator, curli, rpos, rna polymerase, transcription regulator
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
• Cellular location: Cytoplasm : Q7CR52
• Total number of polymer chains: 1
• Total formula weight: 18169.44

Authors

Cavaliere, P.,Levi-Acobas, F.,Monteil, V.,Bellalou, J.,Mayer, C.,Norel, F.,Sizun, C. (deposition date: 2015-02-07, release date: 2015-12-23, Last modification date: 2024-05-15)

Primary citation

Cavaliere, P.,Sizun, C.,Levi-Acobas, F.,Nowakowski, M.,Monteil, V.,Bontems, F.,Bellalou, J.,Mayer, C.,Norel, F.
Binding interface between the Salmonella sigma (S)/RpoS subunit of RNA polymerase and Crl: hints from bacterial species lacking crl.
Sci Rep, 5:13564-13564, 2015

PubMed Abstract: In many Gram-negative bacteria, including Salmonella enterica serovar Typhimurium (S. Typhimurium), the sigma factor RpoS/σ(S) accumulates during stationary phase of growth, and associates with the core RNA polymerase enzyme (E) to promote transcription initiation of genes involved in general stress resistance and starvation survival. Whereas σ factors are usually inactivated upon interaction with anti-σ proteins, σ(S) binding to the Crl protein increases σ(S) activity by favouring its association to E. Taking advantage of evolution of the σ(S) sequence in bacterial species that do not contain a crl gene, like Pseudomonas aeruginosa, we identified and assigned a critical arginine residue in σ(S) to the S. Typhimurium σ(S)-Crl binding interface. We solved the solution structure of S. Typhimurium Crl by NMR and used it for NMR binding assays with σ(S) and to generate in silico models of the σ(S)-Crl complex constrained by mutational analysis. The σ(S)-Crl models suggest that the identified arginine in σ(S) interacts with an aspartate of Crl that is required for σ(S) binding and is located inside a cavity enclosed by flexible loops, which also contribute to the interface. This study provides the basis for further structural investigation of the σ(S)-Crl complex.

PubMed: 26338235
DOI: 10.1038/srep13564

Experimental method

SOLUTION NMR