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4fsc

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==Crystal Structure of Bacillus thuringiensis PlcR in its apo form==
==Crystal Structure of Bacillus thuringiensis PlcR in its apo form==
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<StructureSection load='4fsc' size='340' side='right' caption='[[4fsc]], [[Resolution|resolution]] 3.65&Aring;' scene=''>
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<StructureSection load='4fsc' size='340' side='right'caption='[[4fsc]], [[Resolution|resolution]] 3.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fsc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis_bt407 Bacillus thuringiensis bt407]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FSC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FSC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fsc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis_Bt407 Bacillus thuringiensis Bt407]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FSC FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3u3w|3u3w]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.65&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bthur0002_52210, plcR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=527021 Bacillus thuringiensis Bt407])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fsc OCA], [https://pdbe.org/4fsc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fsc RCSB], [https://www.ebi.ac.uk/pdbsum/4fsc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fsc ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fsc OCA], [http://pdbe.org/4fsc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fsc RCSB], [http://www.ebi.ac.uk/pdbsum/4fsc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fsc ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q45782_BACTU Q45782_BACTU]
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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.
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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<ref>PMID:23277548</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4fsc" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Transcriptional activator|Transcriptional activator]]
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*[[Sandbox 3001|Sandbox 3001]]
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== References ==
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*[[Spike protein 3D structures|Spike protein 3D structures]]
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<references/>
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*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus thuringiensis bt407]]
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[[Category: Bacillus thuringiensis Bt407]]
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[[Category: Bouillaut, L]]
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[[Category: Large Structures]]
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[[Category: Grenha, R]]
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[[Category: Bouillaut L]]
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[[Category: Lereclus, D]]
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[[Category: Grenha R]]
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[[Category: Nessler, S]]
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[[Category: Lereclus D]]
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[[Category: Slamti, L]]
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[[Category: Nessler S]]
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[[Category: Hth dna-binding domain]]
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[[Category: Slamti L]]
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[[Category: Plcr apoform]]
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[[Category: Pleiotropic regulator]]
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[[Category: Quorum sensing]]
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[[Category: Transcription activator]]
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[[Category: Transcriptional activator]]
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Current revision

Crystal Structure of Bacillus thuringiensis PlcR in its apo form

PDB ID 4fsc

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