3u3w: Difference between revisions

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<StructureSection load='3u3w' size='340' side='right'caption='[[3u3w]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3u3w' size='340' side='right'caption='[[3u3w]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3u3w]] is a 6 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=3U3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U3W FirstGlance]. <br>
<table><tr><td colspan='2'>[[3u3w]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus] and [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=3U3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U3W FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">plcR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=527021 Bacillus thuringiensis Bt407])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=3u3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u3w OCA], [https://pdbe.org/3u3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u3w RCSB], [https://www.ebi.ac.uk/pdbsum/3u3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u3w ProSAT]</span></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=3u3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u3w OCA], [https://pdbe.org/3u3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u3w RCSB], [https://www.ebi.ac.uk/pdbsum/3u3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u3w ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q45782_BACTU Q45782_BACTU]
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3u3w" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus thuringiensis bt407]]
[[Category: Bacillus cereus]]
[[Category: Bacillus thuringiensis Bt407]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bouillaut, L]]
[[Category: Bouillaut L]]
[[Category: Grenha, R]]
[[Category: Grenha R]]
[[Category: Lereclus, D]]
[[Category: Lereclus D]]
[[Category: Nessler, S]]
[[Category: Nessler S]]
[[Category: Slamti, L]]
[[Category: Slamti L]]
[[Category: Hth dna-binding domain]]
[[Category: Plcr-papr7-dna]]
[[Category: Pleiotropic regulator]]
[[Category: Quorum sensing]]
[[Category: Ternary complex]]
[[Category: Transcription activator-dna complex]]

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