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PDBsum entry 4gpk
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Transcription, peptide binding protein
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PDB id
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4gpk
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PDB id:
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| Name: |
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Transcription, peptide binding protein
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Title:
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Crystal structure of nprr in complex with its cognate peptide nprx
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Structure:
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Nprr. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Fragment: this is a truncated form of the full-length protein, missing the 60 residues of the n-terminal hth domain, and with an additional c-terminal his-tag. Engineered: yes. Nprx peptide. Chain: m, n, o, p, q, r, s, t, u, v, w, x. Engineered: yes
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Source:
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Bacillus thuringiensis serovar thuringiensis. Organism_taxid: 1432. Gene: nprr. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes
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Resolution:
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3.20Å
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R-factor:
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0.276
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R-free:
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0.299
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Authors:
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S.Zouhir,B.Guimaraes,S.Perchat,M.Nicaise,D.Lereclus,S.Nessler
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Key ref:
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S.Zouhir
et al.
(2013).
Peptide-binding dependent conformational changes regulate the transcriptional activity of the quorum-sensor NprR.
Nucleic Acids Res,
41,
7920-7933.
PubMed id:
DOI:
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Date:
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21-Aug-12
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Release date:
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03-Jul-13
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PROCHECK
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Headers
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References
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G5DDY8
(G5DDY8_BACTU) -
NprR (Fragment) from Bacillus thuringiensis serovar thuringiensis
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Seq:
Struc:
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374 a.a.
343 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Nucleic Acids Res
41:7920-7933
(2013)
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PubMed id:
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Peptide-binding dependent conformational changes regulate the transcriptional activity of the quorum-sensor NprR.
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S.Zouhir,
S.Perchat,
M.Nicaise,
J.Perez,
B.Guimaraes,
D.Lereclus,
S.Nessler.
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ABSTRACT
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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.
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