View source for 6jgf


==Crystal structure of Se-Met CadR from P. putida with a 21 residue C-terminal truncation==
<StructureSection load='6jgf' size='340' side='right'caption='[[6jgf]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jgf]] is a 1 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=6JGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JGF 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]] 2.15&#8491;</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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6jgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jgf OCA], [https://pdbe.org/6jgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jgf RCSB], [https://www.ebi.ac.uk/pdbsum/6jgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jgf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q93TP7_PSEPU Q93TP7_PSEPU] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:31548408</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jgf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Chen H]]
[[Category: Gan JH]]
[[Category: Liu XC]]