4GPK

Crystal structure of NprR in complex with its cognate peptide NprX

Summary for 4GPK

• Entry DOI: 10.2210/pdb4gpk/pdb
• Descriptor: NprR, NprX peptide (2 entities in total)
• Functional Keywords: tpr motif, transcription factor, quorum sensor, transcription-signaling peptide complex, transcription, peptide binding protein
• Biological source: Bacillus thuringiensis serovar thuringiensis
• Total number of polymer chains: 24
• Total formula weight: 544009.36

Authors

Zouhir, S.,Guimaraes, B.,Perchat, S.,Nicaise, M.,Lereclus, D.,Nessler, S. (deposition date: 2012-08-21, release date: 2013-07-03, Last modification date: 2024-02-28)

Primary citation

Zouhir, S.,Perchat, S.,Nicaise, M.,Perez, J.,Guimaraes, B.,Lereclus, D.,Nessler, S.
Peptide-binding dependent conformational changes regulate the transcriptional activity of the quorum-sensor NprR.
Nucleic Acids Res., 41:7920-7933, 2013

PubMed Abstract: 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.

PubMed: 23793817
DOI: 10.1093/nar/gkt546

Experimental method

X-RAY DIFFRACTION (3.2 Å)