7e1b: Difference between revisions
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==Crystal structure of VbrR-DNA complex== | |||
<StructureSection load='7e1b' size='340' side='right'caption='[[7e1b]], [[Resolution|resolution]] 4.59Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7e1b]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_parahaemolyticus Vibrio parahaemolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E1B FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.587Å</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=7e1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e1b OCA], [https://pdbe.org/7e1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e1b RCSB], [https://www.ebi.ac.uk/pdbsum/7e1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e1b ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q87HP4_VIBPA Q87HP4_VIBPA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Two-component systems typically consist of a paired histidine kinase and response regulator and couple environmental changes to adaptive responses. The response regulator VbrR from Vibrio parahaemolyticus, a member of the OmpR/PhoB family, regulates virulence and antibiotic resistance genes. The activation mechanism of VbrR remains unclear. Here, we report the crystal structures of full-length VbrR in complex with DNA in the active conformation and the N-terminal receiver domain (RD) and the C-terminal DNA-binding domain (DBD) in both active and inactive conformations. Structural and biochemical analyses suggest that unphosphorylated VbrR adopts mainly as inactive dimers through the DBD at the autoinhibitory state. The RD undergoes a monomer-to-dimer transition upon phosphorylation, which further induces the transition of DBD from an autoinhibitory dimer to an active dimer and enables its binding with target DNA. Our study suggests a new model for phosphorylation-induced activation of response regulators and sheds light on the pathogenesis of V. parahaemolyticus. | |||
Structural basis of phosphorylation-induced activation of the response regulator VbrR.,Hong S, Guo J, Zhang X, Zhou X, Zhang P, Yu F Acta Biochim Biophys Sin (Shanghai). 2023 Jan 25;55(1):43-50. doi: , 10.3724/abbs.2022200. PMID:36647726<ref>PMID:36647726</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Hong | <div class="pdbe-citations 7e1b" style="background-color:#fffaf0;"></div> | ||
[[Category: Zhang | |||
==See Also== | |||
*[[Response regulator 3D structure|Response regulator 3D structure]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Vibrio parahaemolyticus]] | |||
[[Category: Hong S]] | |||
[[Category: Zhang P]] | |||
[[Category: Zhang X]] | |||
Latest revision as of 22:32, 29 May 2024
Crystal structure of VbrR-DNA complexCrystal structure of VbrR-DNA complex
Structural highlights
FunctionPublication Abstract from PubMedTwo-component systems typically consist of a paired histidine kinase and response regulator and couple environmental changes to adaptive responses. The response regulator VbrR from Vibrio parahaemolyticus, a member of the OmpR/PhoB family, regulates virulence and antibiotic resistance genes. The activation mechanism of VbrR remains unclear. Here, we report the crystal structures of full-length VbrR in complex with DNA in the active conformation and the N-terminal receiver domain (RD) and the C-terminal DNA-binding domain (DBD) in both active and inactive conformations. Structural and biochemical analyses suggest that unphosphorylated VbrR adopts mainly as inactive dimers through the DBD at the autoinhibitory state. The RD undergoes a monomer-to-dimer transition upon phosphorylation, which further induces the transition of DBD from an autoinhibitory dimer to an active dimer and enables its binding with target DNA. Our study suggests a new model for phosphorylation-induced activation of response regulators and sheds light on the pathogenesis of V. parahaemolyticus. Structural basis of phosphorylation-induced activation of the response regulator VbrR.,Hong S, Guo J, Zhang X, Zhou X, Zhang P, Yu F Acta Biochim Biophys Sin (Shanghai). 2023 Jan 25;55(1):43-50. doi: , 10.3724/abbs.2022200. PMID:36647726[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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