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5ku5

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==Crystal Structure of CusS Sensor Domain with Silver Bound==
==Crystal Structure of CusS Sensor Domain with Silver Bound==
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<StructureSection load='5ku5' size='340' side='right' caption='[[5ku5]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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<StructureSection load='5ku5' size='340' side='right'caption='[[5ku5]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ku5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KU5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KU5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ku5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KU5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AG:SILVER+ION'>AG</scene></td></tr>
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</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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AG:SILVER+ION'>AG</scene></td></tr>
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<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=5ku5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ku5 OCA], [http://pdbe.org/5ku5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ku5 RCSB], [http://www.ebi.ac.uk/pdbsum/5ku5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ku5 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ku5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ku5 OCA], [https://pdbe.org/5ku5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ku5 RCSB], [https://www.ebi.ac.uk/pdbsum/5ku5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ku5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CUSS_ECOLI CUSS_ECOLI]] Member of the two-component regulatory system CusS/CusR. Copper ion sensor. Could also be a silver ion sensor. Activates CusR by phosphorylation.<ref>PMID:11004187</ref> <ref>PMID:11399769</ref> <ref>PMID:15522865</ref>
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[https://www.uniprot.org/uniprot/CUSS_ECOLI CUSS_ECOLI] Member of the two-component regulatory system CusS/CusR. Copper ion sensor. Could also be a silver ion sensor. Activates CusR by phosphorylation.<ref>PMID:11004187</ref> <ref>PMID:11399769</ref> <ref>PMID:15522865</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In bacteria, two-component systems act as signaling systems to respond to environmental stimuli. Two-component systems generally consist of a sensor histidine kinase and a response regulator, which work together through histidyl-aspartyl phosphorelay to result in gene regulation. One of the two-component systems in Escherichia coli, CusS-CusR, is known to induce expression of cusCFBA genes at increased periplasmic Cu(I) and Ag(I) concentrations to help maintain metal ion homeostasis. CusS is a membrane-associated histidine kinase with a periplasmic sensor domain connected to the cytoplasmic ATP binding and catalytic domains through two transmembrane helices. The mechanism of how CusS senses increasing metal ion concentrations and activates CusR is not yet known. Here, we present the crystal structure of the Ag(I)-bound periplasmic sensor domain of CusS at a resolution of 2.15 A. The structure reveals that CusS forms a homodimer with four Ag(I) binding sites per dimeric complex. Two symmetric metal binding sites are found at the dimeric interface, which are each formed by two histidines and one phenylalanine with an unusual cation-pi interaction. The other metal ion binding sites are in a nonconserved region within each monomer. Functional analyses of CusS variants with mutations in the metal sites suggest that the metal ion binding site at the dimer interface is more important for function. The structural and functional data provide support for a model in which metal-induced dimerization results in increases in kinase activity in the cytoplasmic domains of CusS.
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The Structure of the Periplasmic Sensor Domain of the Histidine Kinase CusS Shows Unusual Metal Ion Coordination at the Dimeric Interface.,Affandi T, Issaian AV, McEvoy MM Biochemistry. 2016 Sep 12. PMID:27583660<ref>PMID:27583660</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5ku5" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Histidine kinase]]
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[[Category: Escherichia coli K-12]]
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[[Category: Affandi, T]]
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[[Category: Large Structures]]
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[[Category: Issaian, A V]]
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[[Category: Affandi T]]
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[[Category: McEvoy, M M]]
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[[Category: Issaian AV]]
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[[Category: Metal efflux system]]
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[[Category: McEvoy MM]]
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[[Category: Pdc fold]]
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[[Category: Silver binding]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of CusS Sensor Domain with Silver Bound

PDB ID 5ku5

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