2qfc
Crystal Structure of Bacillus thuringiensis PlcR complexed with PapR
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OverviewOverview
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.
About this StructureAbout this Structure
2QFC is a Protein complex structure of sequences from Bacillus thuringiensis with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structure of PlcR: Insights into virulence regulation and evolution of quorum sensing in Gram-positive bacteria., Declerck N, Bouillaut L, Chaix D, Rugani N, Slamti L, Hoh F, Lereclus D, Arold ST, Proc Natl Acad Sci U S A. 2007 Nov 20;104(47):18490-5. Epub 2007 Nov 12. PMID:17998541
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