7dwm: Difference between revisions
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<StructureSection load='7dwm' size='340' side='right'caption='[[7dwm]], [[Resolution|resolution]] 2.65Å' scene=''> | <StructureSection load='7dwm' size='340' side='right'caption='[[7dwm]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7dwm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DWM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DWM FirstGlance]. <br> | <table><tr><td colspan='2'>[[7dwm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_virus_VP882 Vibrio virus VP882]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DWM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DWM FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1U:3,5-dimethylpyrazin-2-ol'>A1U</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]] 2.65Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1U:3,5-dimethylpyrazin-2-ol'>A1U</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=7dwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dwm OCA], [https://pdbe.org/7dwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dwm RCSB], [https://www.ebi.ac.uk/pdbsum/7dwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dwm 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=7dwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dwm OCA], [https://pdbe.org/7dwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dwm RCSB], [https://www.ebi.ac.uk/pdbsum/7dwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dwm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A2I306_9CAUD A2I306_9CAUD] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Vibrio virus VP882]] | ||
[[Category: | [[Category: Gu Y]] | ||
[[Category: | [[Category: Yang WS]] | ||
Latest revision as of 19:41, 29 November 2023
Crystal structure of the phage VqmA-DPO complexCrystal structure of the phage VqmA-DPO complex
Structural highlights
FunctionPublication Abstract from PubMedThe quorum-sensing (QS) system between the phages and their hosts is important for the phage lysis-lysogeny decision. In Vibrio cholerae, the QS system consists of a LuxR-type receptor VqmA (VqmAVc) and an autoinducer molecule 3,5-dimethylpyrazin-2-ol (DPO). A VqmA homolog encoded by vibriophage VP882 (VqmAPhage) can intervene the host QS system via binding to both the host-produced DPO and its cognate promoter (Pqtip) to induce the phage lysogeny-to-lysis transition, whereas VqmAVc cannot influence the VqmAPhage-induced pathway, suggesting an asymmetry regulation. In this study, we report the crystal structure of VqmAPhage-DPO complex at 2.65 A and reveal that the mechanism of DPO recognition is conserved in VqmA homologs. Besides, we identify a non-classical palindrome sequence in Pqtip, which can be effectively recognized by VqmAPhage but not VqmAVc. The sequence contains an interval longer than that in the vqmR promoter recognized by VqmAVc. In addition, the two DBD regions in the VqmAPhage dimer exhibit more relaxed architecture than that of the reported VqmAVc, which is likely to be in the conformation that may easily bind to target promoter containing a longer interval. In summary, our findings provide a structural and biochemical basis for the DBD-dependent DNA recognition in different promoter regions in the phage lysogeny-to-lysis decision communication system, and provide clues for developing phage therapies against Vibrio cholerae infection. Understanding the mechanism of asymmetric gene regulation determined by the VqmA of vibriophage.,Gu Y, Zhi SX, Yang N, Yang WS Biochem Biophys Res Commun. 2021 Apr 22;558:51-56. doi:, 10.1016/j.bbrc.2021.04.036. PMID:33895551[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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