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| | <StructureSection load='4ua2' size='340' side='right'caption='[[4ua2]], [[Resolution|resolution]] 2.61Å' scene=''> | | <StructureSection load='4ua2' size='340' side='right'caption='[[4ua2]], [[Resolution|resolution]] 2.61Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ua2]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UA2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UA2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ua2]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UA2 FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ua1|4ua1]]</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=4ua2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ua2 OCA], [https://pdbe.org/4ua2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ua2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ua2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ua2 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">merR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</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=4ua2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ua2 OCA], [http://pdbe.org/4ua2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ua2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ua2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ua2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q799U3_PRIMG Q799U3_PRIMG] Mediates the mercuric-dependent induction of mercury resistance operon. In the absence of mercury MerR represses transcription by binding tightly to the mer operator region; when mercury is present the dimeric complex binds a single ion and becomes a potent transcriptional activator, while remaining bound to the mer site.[ARBA:ARBA00024874] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4ua2" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4ua2" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 14581]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chan, N L]] | + | [[Category: Priestia megaterium]] |
| - | [[Category: Chang, C C]] | + | [[Category: Chan NL]] |
| - | [[Category: Huang, C C]] | + | [[Category: Chang CC]] |
| - | [[Category: Lin, L Y]] | + | [[Category: Huang CC]] |
| - | [[Category: Zou, X W]] | + | [[Category: Lin LY]] |
| - | [[Category: Dna binding protein]] | + | [[Category: Zou XW]] |
| - | [[Category: Metalloregulatory protein]]
| + | |
| Structural highlights
Function
Q799U3_PRIMG Mediates the mercuric-dependent induction of mercury resistance operon. In the absence of mercury MerR represses transcription by binding tightly to the mer operator region; when mercury is present the dimeric complex binds a single ion and becomes a potent transcriptional activator, while remaining bound to the mer site.[ARBA:ARBA00024874]
Publication Abstract from PubMed
The mer operon confers bacterial resistance to inorganic mercury (Hg2+) and organomercurials by encoding proteins involved in sensing, transport and detoxification of these cytotoxic agents. Expression of the mer operon is under tight control by the dual-function transcriptional regulator MerR. The metal-free, apo MerR binds to the mer operator/promoter region as a repressor to block transcription initiation, but is converted into an activator upon Hg2+-binding. To understand how MerR interacts with Hg2+ and how Hg2+-binding modulates MerR function, we report here the crystal structures of apo and Hg2+-bound MerR from Bacillus megaterium, corresponding respectively to the repressor and activator conformation of MerR. To our knowledge, the apo-MerR structure represents the first visualization of a MerR family member in its intact and inducer-free form. And the Hg2+-MerR structure offers the first view of a triligated Hg2+-thiolate center in a metalloprotein, confirming that MerR binds Hg2+ via trigonal planar coordination geometry. Structural comparison revealed the conformational transition of MerR is coupled to the assembly/disassembly of a buried Hg2+ binding site, thereby providing a structural basis for the Hg2+-mediated functional switching of MerR. The pronounced Hg2+-induced repositioning of the MerR DNA-binding domains suggests a plausible mechanism for the transcriptional regulation of the mer operon.
Structural basis of the mercury(II)-mediated conformational switching of the dual-function transcriptional regulator MerR.,Chang CC, Lin LY, Zou XW, Huang CC, Chan NL Nucleic Acids Res. 2015 Jul 6. pii: gkv681. PMID:26150423[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chang CC, Lin LY, Zou XW, Huang CC, Chan NL. Structural basis of the mercury(II)-mediated conformational switching of the dual-function transcriptional regulator MerR. Nucleic Acids Res. 2015 Jul 6. pii: gkv681. PMID:26150423 doi:http://dx.doi.org/10.1093/nar/gkv681
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