4GPK

Crystal structure of NprR in complex with its cognate peptide NprX

4GPK の概要

• エントリーDOI: 10.2210/pdb4gpk/pdb
• 分子名称: NprR, NprX peptide (2 entities in total)
• 機能のキーワード: tpr motif, transcription factor, quorum sensor, transcription-signaling peptide complex, transcription, peptide binding protein
• 由来する生物種: Bacillus thuringiensis serovar thuringiensis
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 544009.36

構造登録者

Zouhir, S.,Guimaraes, B.,Perchat, S.,Nicaise, M.,Lereclus, D.,Nessler, S. (登録日: 2012-08-21, 公開日: 2013-07-03, 最終更新日: 2024-02-28)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.2 Å)