6hp5
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==ARBITRIUM PEPTIDE RECEPTOR FROM SPBETA PHAGE== | |
| + | <StructureSection load='6hp5' size='340' side='right' caption='[[6hp5]], [[Resolution|resolution]] 2.28Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6hp5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HP5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HP5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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='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=6hp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hp5 OCA], [http://pdbe.org/6hp5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hp5 RCSB], [http://www.ebi.ac.uk/pdbsum/6hp5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hp5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacillus phages use a communication system, termed "arbitrium," to coordinate lysis-lysogeny decisions. Arbitrium communication is mediated by the production and secretion of a hexapeptide (AimP) during lytic cycle. Once internalized, AimP reduces the expression of the negative regulator of lysogeny, AimX, by binding to the transcription factor, AimR, promoting lysogeny. We have elucidated the crystal structures of AimR from the Bacillus subtilis SPbeta phage in its apo form, bound to its DNA operator and in complex with AimP. AimR presents intrinsic plasticity, sharing structural features with the RRNPP quorum-sensing family. Remarkably, AimR binds to an unusual operator with a long spacer that interacts nonspecifically with the receptor TPR domain, while the HTH domain canonically recognizes two inverted repeats. AimP stabilizes a compact conformation of AimR that approximates the DNA-recognition helices, preventing AimR binding to the aimX promoter region. Our results establish the molecular basis of the arbitrium communication system. | ||
| - | + | Deciphering the Molecular Mechanism Underpinning Phage Arbitrium Communication Systems.,Gallego Del Sol F, Penades JR, Marina A Mol Cell. 2019 Feb 6. pii: S1097-2765(19)30045-0. doi:, 10.1016/j.molcel.2019.01.025. PMID:30745087<ref>PMID:30745087</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 6hp5" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Marina, A]] | [[Category: Marina, A]] | ||
| + | [[Category: Sol, F Gallego del]] | ||
| + | [[Category: Arbitrium peptide receptor]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: Spbeta phage]] | ||
Revision as of 06:45, 21 February 2019
ARBITRIUM PEPTIDE RECEPTOR FROM SPBETA PHAGE
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