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| | ==Crystal structure of AimR from Bacillus phage SPbeta in complex with its signalling peptide== | | ==Crystal structure of AimR from Bacillus phage SPbeta in complex with its signalling peptide== |
| - | <StructureSection load='5y24' size='340' side='right' caption='[[5y24]], [[Resolution|resolution]] 1.92Å' scene=''> | + | <StructureSection load='5y24' size='340' side='right'caption='[[5y24]], [[Resolution|resolution]] 1.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5y24]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpspb Bpspb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y24 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y24 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5y24]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_virus_SPbeta Bacillus virus SPbeta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y24 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</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]] 1.922Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aimR, yopK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=66797 BPSPB])</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=5y24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y24 OCA], [https://pdbe.org/5y24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y24 RCSB], [https://www.ebi.ac.uk/pdbsum/5y24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y24 ProSAT]</span></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=5y24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y24 OCA], [http://pdbe.org/5y24 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y24 RCSB], [http://www.ebi.ac.uk/pdbsum/5y24 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y24 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AIMR_BPSPB AIMR_BPSPB]] Transcriptional regulator which is part of the latency-replication switch system that decides at the onset of infection whether to replicate and lyse the host or to lysogenize (latency) and keep the host viable. Activates the transcription of the aimX locus. Transcriptional activation of aimX seems to lead to the productive viral replication (lytic cycle), aimX possibly acting as a regulatory non-coding RNA.[UniProtKB:P0DOE3] | + | [https://www.uniprot.org/uniprot/AIMR_BPSPB AIMR_BPSPB] Transcriptional regulator which is part of the latency-replication switch system that decides at the onset of infection whether to replicate and lyse the host or to lysogenize (latency) and keep the host viable. Activates the transcription of the aimX locus. Transcriptional activation of aimX seems to lead to the productive viral replication (lytic cycle), aimX possibly acting as a regulatory non-coding RNA.[UniProtKB:P0DOE3] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpspb]] | + | [[Category: Bacillus virus SPbeta]] |
| - | [[Category: Guan, Z Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Wang, Q]] | + | [[Category: Guan ZY]] |
| - | [[Category: Yin, P]] | + | [[Category: Wang Q]] |
| - | [[Category: Zou, T T]] | + | [[Category: Yin P]] |
| - | [[Category: Complex with peptide]] | + | [[Category: Zou TT]] |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Peptide binding protein]]
| + | |
| Structural highlights
Function
AIMR_BPSPB Transcriptional regulator which is part of the latency-replication switch system that decides at the onset of infection whether to replicate and lyse the host or to lysogenize (latency) and keep the host viable. Activates the transcription of the aimX locus. Transcriptional activation of aimX seems to lead to the productive viral replication (lytic cycle), aimX possibly acting as a regulatory non-coding RNA.[UniProtKB:P0DOE3]
Publication Abstract from PubMed
A bacteriophage can replicate and release virions from a host cell in the lytic cycle or switch to a lysogenic process in which the phage integrates itself into the host genome as a prophage. In Bacillus cells, some types of phages employ the arbitrium communication system, which contains an arbitrium hexapeptide, the cellular receptor AimR and the lysogenic negative regulator AimX. This system controls the decision between the lytic and lysogenic cycles. However, both the mechanism of molecular recognition between the arbitrium peptide and AimR and how downstream gene expression is regulated remain unknown. Here, we report crystal structures for AimR from the SPbeta phage in the apo form and the arbitrium peptide-bound form at 2.20 A and 1.92 A, respectively. With or without the peptide, AimR dimerizes through the C-terminal capping helix. AimR assembles a superhelical fold and accommodates the peptide encircled by its tetratricopeptide repeats, which is reminiscent of RRNPP family members from the quorum-sensing system. In the absence of the arbitrium peptide, AimR targets the upstream sequence of the aimX gene; its DNA binding activity is prevented following peptide binding. In summary, our findings provide a structural basis for peptide recognition in the phage lysis-lysogeny decision communication system.
Structural basis of the arbitrium peptide-AimR communication system in the phage lysis-lysogeny decision.,Wang Q, Guan Z, Pei K, Wang J, Liu Z, Yin P, Peng D, Zou T Nat Microbiol. 2018 Sep 17. pii: 10.1038/s41564-018-0239-y. doi:, 10.1038/s41564-018-0239-y. PMID:30224798[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang Q, Guan Z, Pei K, Wang J, Liu Z, Yin P, Peng D, Zou T. Structural basis of the arbitrium peptide-AimR communication system in the phage lysis-lysogeny decision. Nat Microbiol. 2018 Sep 17. pii: 10.1038/s41564-018-0239-y. doi:, 10.1038/s41564-018-0239-y. PMID:30224798 doi:http://dx.doi.org/10.1038/s41564-018-0239-y
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