PDBsum entry 2qfc

Transcription regulation

PDB id: 2qfc

Contents

Protein chains

284 a.a. *

Ligands

LEU-PRO-PHE-GLU-PHE ×2

PEG ×4

Waters ×30

* Residue conservation analysis

PDB id:

2qfc

Name:

Transcription regulation

Title:

Crystal structure of bacillus thuringiensis plcr complexed with papr

Structure:

Plcr protein. Chain: a, b. Engineered: yes. C-terminus pentapeptide from papr protein. Chain: c, d. Engineered: yes

Source:

Bacillus thuringiensis serovar israelensis atcc 35646. Organism_taxid: 339854. Strain: serovar israelensis atcc 35646. Gene: plcr. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: synthetic peptide derived from thE C-terminus of papr

Resolution:

2.60Å R-factor: 0.228 R-free: 0.304

Authors:

N.Declerck,D.Chaix,N.Rugani,F.Hoh,S.T.Arold

Key ref:

N.Declerck et al. (2007). Structure of PlcR: Insights into virulence regulation and evolution of quorum sensing in Gram-positive bacteria. Proc Natl Acad Sci U S A, 104, 18490-18495. PubMed id: 17998541 DOI: 10.1073/pnas.0704501104

Date:

27-Jun-07 Release date: 06-Nov-07

Protein chains

Q45782  (Q45782_BACTU) -  PlcR protein from Bacillus thuringiensis

Seq: 285 a.a.

Struc: 284 a.a.

DOI no: 10.1073/pnas.0704501104

Proc Natl Acad Sci U S A 104:18490-18495 (2007)

PubMed id: 17998541

Structure of PlcR: Insights into virulence regulation and evolution of quorum sensing in Gram-positive bacteria.

N.Declerck, L.Bouillaut, D.Chaix, N.Rugani, L.Slamti, F.Hoh, D.Lereclus, S.T.Arold.

ABSTRACT

Gram-positive bacteria use a wealth of extracellular signaling peptides, so-called autoinducers, to regulate gene expression according to population densities. These "quorum sensing" systems control vital processes such as virulence, sporulation, and gene transfer. Using x-ray analysis, we determined the structure of PlcR, the major virulence regulator of the Bacillus cereus group, and obtained mechanistic insights into the effects of autoinducer binding. Our structural and phylogenetic analysis further suggests that all of those quorum sensors that bind directly to their autoinducer peptide derive from a common ancestor and form a single family (the RNPP family, for Rap/NprR/PlcR/PrgX) with conserved features. As a consequence, fundamentally different processes in different bacterial genera appear regulated by essentially the same autoinducer recognition mechanism. Our results shed light on virulence control by PlcR and elucidate origin and evolution of multicellular behavior in bacteria.

Selected figure(s)

Figure 1.
Fig. 1. Structure of PapR5:PlcR and comparison to cCF10:PrgX. Shown are ribbon presentations of PapR5:PlcR (A) and cCF10:PrgX (B) [Protein Data Bank entry 2AXZ (9)]. Chains A and B of PlcR and PrgX are colored in magenta and cyan, with their respective HTH domains in dark gray and dark blue. Helix 3 of the HTH domains that inserts into the major DNA groove is colored in red. The C-terminal extension of PrgX is colored in light gray. Ligand peptides are shown in yellow and green. Left and Right represent 90° views. (C and D) Close-up views of the peptide–protein interactions for PapR:PlcR (C) and cCF10:PrgX (D). Oligopeptides are yellow, and key residues are labeled. Unbiased 3F[o]–2F[c] electron density for PapR5 is shown in gray. Hydrogen bonds between cCF10 and PrgX key residues are indicated by black lines.

Figure 4.
Fig. 4. Molecular effects of peptide recognition. (A) The curvature of the PrgX TPR-like domain increases upon autoinducer binding. Cyan, apo-PrgX (Protein Data Bank entry 2AXU); magenta, cCF10:PrgX (Protein Data Bank entry 2AXZ). The pheromone (yellow) is shown in stick representation. (B) Drawing illustrating how the increased TPR domain curvature in PapR:PlcR may rearrange the HTH domains. (Lower) apo-PlcR. (Upper) PapR:PlcR.

Figures were selected by an automated process.