3u3w

Crystal Structure of Bacillus thuringiensis PlcR in complex with the peptide PapR7 and DNACrystal Structure of Bacillus thuringiensis PlcR in complex with the peptide PapR7 and DNA

Structural highlights 3u3w is a 6 chain structure with sequence from Bacillus thuringiensis bt407. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Gene: plcR (Bacillus thuringiensis Bt407) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The quorum-sensing regulator PlcR is the master regulator of most known virulence factors in Bacillus cereus. It is a helix-turn-helix (HTH)-type transcription factor activated upon binding of its cognate signaling peptide PapR on a tetratricopeptide repeat-type regulatory domain. The structural and functional properties of PlcR have defined a new family of sensor regulators, called the RNPP family (for Rap, NprR, PrgX, and PlcR), in Gram-positive bacteria. To fully understand the activation mechanism of PlcR, we took a closer look at the conformation changes induced upon binding of PapR and of its target DNA, known as PlcR-box. For that purpose we have determined the structures of the apoform of PlcR (Apo PlcR) and of the ternary complex of PlcR with PapR and the PlcR-box from the plcA promoter. Comparison of the apoform of PlcR with the previously published structure of the PlcR-PapR binary complex shows how a small conformational change induced in the C-terminal region of the tetratricopeptide repeat (TPR) domain upon peptide binding propagates via the linker helix to the N-terminal HTH DNA-binding domain. Further comparison with the PlcR-PapR-DNA ternary complex shows how the activation of the PlcR dimer allows the linker helix to undergo a drastic conformational change and subsequent proper positioning of the HTH domains in the major groove of the two half sites of the pseudopalindromic PlcR-box. Together with random mutagenesis experiments and interaction measurements using peptides from distinct pherogroups, this structural analysis allows us to propose a molecular mechanism for this functional switch. Structural basis for the activation mechanism of the PlcR virulence regulator by the quorum-sensing signal peptide PapR.,Grenha R, Slamti L, Nicaise M, Refes Y, Lereclus D, Nessler S Proc Natl Acad Sci U S A. 2013 Jan 15;110(3):1047-52. doi:, 10.1073/pnas.1213770110. Epub 2012 Dec 31. PMID:23277548 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transcriptional activator

spinqualitylabelsall models 3u3w, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image