4gpk

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gpk OCA], [https://pdbe.org/4gpk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gpk RCSB], [https://www.ebi.ac.uk/pdbsum/4gpk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gpk ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The transcriptional regulator NprR controls the expression of genes essential for the adaptative response of Bacillus cereus. NprR belongs to the RNPP family of directly regulated quorum sensors from Gram-positive bacteria. It is activated by the re-imported signaling peptide NprX. To elucidate the activation mechanism of this quorum-sensing system, we analyzed the conformation changes induced on binding of NprX. We solved the crystal structure of the NprR/NprX binary complex and characterized the apo form of NprR in solution. We demonstrated that apo NprR is a dimer that switches to a tetramer in the presence of NprX. Mutagenesis, and functional analysis allowed us to identify the protein and peptide residues directly involved in the NprR activation process. Based on the comparison with the Rap proteins, we propose a model for the peptide-induced conformational change allowing the apo dimer to switch to an active tetramer specifically recognizing target DNA sequences.

Peptide-binding dependent conformational changes regulate the transcriptional activity of the quorum-sensor NprR.,Zouhir S, Perchat S, Nicaise M, Perez J, Guimaraes B, Lereclus D, Nessler S Nucleic Acids Res. 2013 Jun 22. PMID:23793817<ref>PMID:23793817</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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