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==The Crystal structure of HucR mutant (HucR-E48Q) from Deinococcus radiodurans== | ==The Crystal structure of HucR mutant (HucR-E48Q) from Deinococcus radiodurans== | ||
<StructureSection load='5dd8' size='340' side='right' caption='[[5dd8]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='5dd8' size='340' side='right'caption='[[5dd8]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5dd8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DD8 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5dd8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DD8 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.05Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=5dd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dd8 OCA], [https://pdbe.org/5dd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dd8 RCSB], [https://www.ebi.ac.uk/pdbsum/5dd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dd8 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9RV71_DEIRA Q9RV71_DEIRA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Therapeutic strategies have been reported that depend on synthetic network devices in which a urate-sensing transcriptional regulator detects pathological levels of urate and triggers production or release of urate oxidase. The transcription factor involved, HucR, is a member of the multiple antibiotic resistance (MarR) protein family. We show that protonation of stacked histidine residues at the pivot point of long helices that form the scaffold of the dimer interface leads to reversible formation of a molten globule state and significantly attenuated DNA binding at physiological temperatures. We also show that binding of urate to symmetrical sites in each protein lobe is communicated via the dimer interface. This is the first demonstration of regulation of a MarR family transcription factor by pH-dependent interconversion between a molten globule and a compact folded state. Our data further suggest that HucR may be utilized in synthetic devices that depend on detection of pH changes. | |||
Histidine switch controlling pH-dependent protein folding and DNA binding in a transcription factor at the core of synthetic network devices.,Deochand DK, Perera IC, Crochet RB, Gilbert NC, Newcomer ME, Grove A Mol Biosyst. 2016 Jul 19;12(8):2417-26. doi: 10.1039/c6mb00304d. PMID:27282811<ref>PMID:27282811</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5dd8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Deinococcus radiodurans]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Crochet RB]] | ||
[[Category: | [[Category: Deochand DK]] | ||
[[Category: | [[Category: Gilbert NC]] | ||
[[Category: | [[Category: Grove A]] | ||
[[Category: | [[Category: Newcomer ME]] | ||
[[Category: | [[Category: Perera IC]] | ||
Latest revision as of 11:45, 27 September 2023
The Crystal structure of HucR mutant (HucR-E48Q) from Deinococcus radioduransThe Crystal structure of HucR mutant (HucR-E48Q) from Deinococcus radiodurans
Structural highlights
FunctionPublication Abstract from PubMedTherapeutic strategies have been reported that depend on synthetic network devices in which a urate-sensing transcriptional regulator detects pathological levels of urate and triggers production or release of urate oxidase. The transcription factor involved, HucR, is a member of the multiple antibiotic resistance (MarR) protein family. We show that protonation of stacked histidine residues at the pivot point of long helices that form the scaffold of the dimer interface leads to reversible formation of a molten globule state and significantly attenuated DNA binding at physiological temperatures. We also show that binding of urate to symmetrical sites in each protein lobe is communicated via the dimer interface. This is the first demonstration of regulation of a MarR family transcription factor by pH-dependent interconversion between a molten globule and a compact folded state. Our data further suggest that HucR may be utilized in synthetic devices that depend on detection of pH changes. Histidine switch controlling pH-dependent protein folding and DNA binding in a transcription factor at the core of synthetic network devices.,Deochand DK, Perera IC, Crochet RB, Gilbert NC, Newcomer ME, Grove A Mol Biosyst. 2016 Jul 19;12(8):2417-26. doi: 10.1039/c6mb00304d. PMID:27282811[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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