|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal Structure of Bacillus thuringiensis PlcR in its apo form== | | ==Crystal Structure of Bacillus thuringiensis PlcR in its apo form== |
| - | <StructureSection load='4fsc' size='340' side='right' caption='[[4fsc]], [[Resolution|resolution]] 3.65Å' scene=''> | + | <StructureSection load='4fsc' size='340' side='right'caption='[[4fsc]], [[Resolution|resolution]] 3.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <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> | + | <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> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3u3w|3u3w]]</td></tr> | + | </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=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> |
| - | <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>
| + | |
| - | <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> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q45782_BACTU Q45782_BACTU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 19: |
Line 19: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Transcriptional activator|Transcriptional activator]] | + | *[[Sandbox 3001|Sandbox 3001]] |
| | + | *[[Spike protein|Spike protein]] |
| | + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus thuringiensis bt407]] | + | [[Category: Bacillus thuringiensis Bt407]] |
| - | [[Category: Bouillaut, L]] | + | [[Category: Large Structures]] |
| - | [[Category: Grenha, R]] | + | [[Category: Bouillaut L]] |
| - | [[Category: Lereclus, D]] | + | [[Category: Grenha R]] |
| - | [[Category: Nessler, S]] | + | [[Category: Lereclus D]] |
| - | [[Category: Slamti, L]] | + | [[Category: Nessler S]] |
| - | [[Category: Hth dna-binding domain]]
| + | [[Category: Slamti L]] |
| - | [[Category: Plcr apoform]]
| + | |
| - | [[Category: Pleiotropic regulator]]
| + | |
| - | [[Category: Quorum sensing]]
| + | |
| - | [[Category: Transcription activator]]
| + | |
| - | [[Category: Transcriptional activator]]
| + | |
| Structural highlights
Function
Q45782_BACTU
Publication Abstract from PubMed
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Grenha R, Slamti L, Nicaise M, Refes Y, Lereclus D, Nessler S. Structural basis for the activation mechanism of the PlcR virulence regulator by the quorum-sensing signal peptide PapR. 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 doi:http://dx.doi.org/10.1073/pnas.1213770110
|
