2QFC

Crystal Structure of Bacillus thuringiensis PlcR complexed with PapR

Summary for 2QFC

• Entry DOI: 10.2210/pdb2qfc/pdb
• Descriptor: PlcR protein, C-terminus pentapeptide from PapR protein, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: tpr; hth, transcription regulation
• Biological source: Bacillus thuringiensis serovar israelensis ATCC 35646; More
• Total number of polymer chains: 4
• Total formula weight: 71850.55

Authors

Declerck, N.,Chaix, D.,Rugani, N.,Hoh, F.,Arold, S.T. (deposition date: 2007-06-27, release date: 2007-11-06, Last modification date: 2024-02-21)

Primary citation

Declerck, N.,Bouillaut, L.,Chaix, D.,Rugani, N.,Slamti, L.,Hoh, F.,Lereclus, D.,Arold, S.T.
Structure of PlcR: Insights into virulence regulation and evolution of quorum sensing in Gram-positive bacteria
Proc.Natl.Acad.Sci.Usa, 104:18490-18495, 2007

PubMed 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.

PubMed: 17998541
DOI: 10.1073/pnas.0704501104

Experimental method

X-RAY DIFFRACTION (2.6 Å)