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| | <StructureSection load='6jni' size='340' side='right'caption='[[6jni]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='6jni' size='340' side='right'caption='[[6jni]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6jni]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JNI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JNI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6jni]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JNI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JNI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cadR, BIW19_10095, BL240_26950 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6jni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jni OCA], [http://pdbe.org/6jni PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jni RCSB], [http://www.ebi.ac.uk/pdbsum/6jni PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jni 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=6jni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jni OCA], [https://pdbe.org/6jni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jni RCSB], [https://www.ebi.ac.uk/pdbsum/6jni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jni ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q93TP7_PSEPU Q93TP7_PSEPU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus fluorescens putidus flugge 1886]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, H]] | + | [[Category: Pseudomonas putida]] |
| - | [[Category: Gan, J H]] | + | [[Category: Chen H]] |
| - | [[Category: Liu, X C]] | + | [[Category: Gan JH]] |
| - | [[Category: Cadmium regulator]] | + | [[Category: Liu XC]] |
| - | [[Category: Cadr]]
| + | |
| - | [[Category: Merr family]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription-dna complex]]
| + | |
| Structural highlights
Function
Q93TP7_PSEPU
Publication Abstract from PubMed
Detoxification of the highly toxic cadmium element is essential for the survival of living organisms. Pseudomonas putida CadR, a MerR family transcriptional regulator, has been reported to exhibit an ultraspecific response to the cadmium ion. Our crystallographic and spectroscopic studies reveal that the extra cadmium selectivity of CadR is mediated by the unexpected cooperation of thiolate-rich site I and histidine-rich site II. Cadmium binding in site I mediates the reorientation of protein domains and facilitates the assembly of site II. Subsequently, site II bridge-links 2 DNA binding domains through ligands His140/His145 in the C-terminal histidine-rich tail. With dynamic transit between 2 conformational states, this bridge could stabilize the regulator into an optimal conformation that is critical for enhancing the transcriptional activity of the cadmium detoxification system. Our results provide dynamic insight into how nature utilizes the unique cooperative binding mechanism in multisite proteins to recognize cadmium ions specifically.
Selective cadmium regulation mediated by a cooperative binding mechanism in CadR.,Liu X, Hu Q, Yang J, Huang S, Wei T, Chen W, He Y, Wang D, Liu Z, Wang K, Gan J, Chen H Proc Natl Acad Sci U S A. 2019 Oct 8;116(41):20398-20403. doi:, 10.1073/pnas.1908610116. Epub 2019 Sep 23. PMID:31548408[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu X, Hu Q, Yang J, Huang S, Wei T, Chen W, He Y, Wang D, Liu Z, Wang K, Gan J, Chen H. Selective cadmium regulation mediated by a cooperative binding mechanism in CadR. Proc Natl Acad Sci U S A. 2019 Oct 8;116(41):20398-20403. doi:, 10.1073/pnas.1908610116. Epub 2019 Sep 23. PMID:31548408 doi:http://dx.doi.org/10.1073/pnas.1908610116
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