PDBsum entry 6eo2

DNA binding protein

PDB id: 6eo2

Contents

Protein chain

208 a.a.

Waters ×12

PDB id:

6eo2

Name:

DNA binding protein

Title:

Conformational dynamism for DNA interaction in salmonella typhimurium rcsb response regulator. S207c crossed

Structure:

Transcriptional regulatory protein rcsb. Chain: a. Engineered: yes. Other_details: some side chains could not be traced, thus, they remain at ala at residues: m1, e28, e139, k140, i141, s142, d148, k149, r150, k180, v208.

Source:

Salmonella enterica subsp. Enterica serovar typhimurium. Organism_taxid: 90371. Gene: rcsb, stm2270. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.60Å R-factor: 0.221 R-free: 0.246

Authors:

P.Casino,A.Marina

Key ref:

P.Casino et al. (2018). Conformational dynamism for DNA interaction in the Salmonella RcsB response regulator. Nucleic Acids Res, 46, 456-472. PubMed id: 29186528

Date:

08-Oct-17 Release date: 15-Nov-17

Protein chain

P58663  (RCSB_SALTY) -  Transcriptional regulatory protein RcsB from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

Seq: 216 a.a.

Struc: 208 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Nucleic Acids Res 46:456-472 (2018)

PubMed id: 29186528

Conformational dynamism for DNA interaction in the Salmonella RcsB response regulator.

P.Casino, L.Miguel-Romero, J.Huesa, P.García, F.García-Del Portillo, A.Marina.

ABSTRACT

The RcsCDB phosphorelay system controls an extremely large regulon in Enterobacteriaceae that involves processes such as biofilm formation, flagella production, synthesis of extracellular capsules and cell division. Therefore, fine-tuning of this system is essential for virulence in pathogenic microorganisms of this group. The final master effector of the RcsCDB system is the response regulator (RR) RcsB, which activates or represses multiple genes by binding to different promoter regions. This regulatory activity of RcsB can be done alone or in combination with additional transcriptional factors in phosphorylated or dephosphorylated states. The capacity of RcsB to interact with multiple promoters and partners, either dephosphorylated or phosphorylated, suggests an extremely conformational dynamism for this RR. To shed light on the activation mechanism of RcsB and its implication on promoter recognition, we solved the crystal structure of full-length RcsB from Salmonella enterica serovar Typhimurium in the presence and absence of a phosphomimetic molecule BeF3-. These two novel structures have guided an extensive site-directed mutagenesis study at the structural and functional level that confirms RcsB conformational plasticity and dynamism. Our data allowed us to propose a β5-T switch mechanism where phosphorylation is coupled to alternative DNA binding ways and which highlights the conformational dynamism of RcsB to be so pleiotropic.