PDBsum entry 2mz8

Transcription regulator

PDB id: 2mz8

Contents

Protein chain

133 a.a.

PDB id:

2mz8

Name:

Transcription regulator

Title:

Solution nmr structure of salmonella typhimurium transcriptional regulator protein crl

Structure:

Sigma factor-binding protein crl. Chain: a. Engineered: yes

Source:

Salmonella enterica subsp. Enterica serovar typhimurium str. Lt2. Organism_taxid: 99287. Strain: lt2 / sgsc1412 / atcc 700720. Atcc: 14028. Gene: crl, stm0319. Expressed in: escherichia coli. Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

P.Cavaliere,F.Levi-Acobas,V.Monteil,J.Bellalou,C.Mayer,F.Norel, C.Sizun

Key ref:

P.Cavaliere et al. (2015). Binding interface between the Salmonella σ(S)/RpoS subunit of RNA polymerase and Crl: hints from bacterial species lacking crl. Sci Rep, 5, 13564. PubMed id: 26338235 DOI: 10.1038/srep13564

Date:

07-Feb-15 Release date: 23-Dec-15

Protein chain

Q7CR52  (CRL_SALTY) -  Sigma factor-binding protein Crl from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

Seq: 133 a.a.

Struc: 133 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/srep13564

Sci Rep 5:13564 (2015)

PubMed id: 26338235

Binding interface between the Salmonella σ(S)/RpoS subunit of RNA polymerase and Crl: hints from bacterial species lacking crl.

P.Cavaliere, C.Sizun, F.Levi-Acobas, M.Nowakowski, V.Monteil, F.Bontems, J.Bellalou, C.Mayer, F.Norel.

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.