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2k0q

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Revision as of 10:24, 18 July 2018

Solution structure of CopK, a periplasmic protein involved in copper resistance in Cupriavidus metallidurans CH34

Structural highlights

2k0q is a 1 chain structure with sequence from Cupriavidus metallidurans. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	copK (CUPRIAVIDUS METALLIDURANS)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[COPK_RALME] Involved in resistance to copper. Can bind up to 2 copper ions. Has higher affinity for Cu(+) than for Cu(2+).^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The copK gene is localized on the pMOL30 plasmid of Cupriavidus metallidurans CH34 within the complex cop cluster of genes, for which 21 genes have been identified. The expression of the corresponding periplasmic CopK protein is strongly upregulated in the presence of copper, leading to a high periplasmic accumulation. The structure and metal-binding properties of CopK were investigated by NMR and mass spectrometry. The protein is dimeric in the apo state with a dissociation constant in the range of 10(-5) M estimated from analytical ultracentrifugation. Mass spectrometry revealed that CopK has two high-affinity Cu(I)-binding sites per monomer with different Cu(I) affinities. Binding of Cu(II) was observed but appeared to be non-specific. The solution structure of apo-CopK revealed an all-beta fold formed of two beta-sheets in perpendicular orientation with an unstructured C-terminal tail. The dimer interface is formed by the surface of the C-terminal beta-sheet. Binding of the first Cu(I)-ion induces a major structural modification involving dissociation of the dimeric apo-protein. Backbone chemical shifts determined for the 1Cu(I)-bound form confirm the conservation of the N-terminal beta-sheet, while the last strand of the C-terminal sheet appears in slow conformational exchange. We hypothesize that the partial disruption of the C-terminal beta-sheet is related to dimer dissociation. NH-exchange data acquired on the apo-protein are consistent with a lower thermodynamic stability of the C-terminal sheet. CopK contains seven methionine residues, five of which appear highly conserved. Chemical shift data suggest implication of two or three methionines (Met54, Met38, Met28) in the first Cu(I) site. Addition of a second Cu(I) ion further increases protein plasticity. Comparison of the structural and metal-binding properties of CopK with other periplasmic copper-binding proteins reveals two conserved features within these functionally related proteins: the all-beta fold and the methionine-rich Cu(I)-binding site.

Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge.,Bersch B, Favier A, Schanda P, van Aelst S, Vallaeys T, Coves J, Mergeay M, Wattiez R J Mol Biol. 2008 Jul 4;380(2):386-403. Epub 2008 May 15. PMID:18533181^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bersch B, Favier A, Schanda P, van Aelst S, Vallaeys T, Coves J, Mergeay M, Wattiez R. Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge. J Mol Biol. 2008 Jul 4;380(2):386-403. Epub 2008 May 15. PMID:18533181 doi:10.1016/j.jmb.2008.05.017
↑ Bersch B, Favier A, Schanda P, van Aelst S, Vallaeys T, Coves J, Mergeay M, Wattiez R. Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge. J Mol Biol. 2008 Jul 4;380(2):386-403. Epub 2008 May 15. PMID:18533181 doi:10.1016/j.jmb.2008.05.017

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2k0q"

@@ Line 1: / Line 1: @@
 ==Solution structure of CopK, a periplasmic protein involved in copper resistance in Cupriavidus metallidurans CH34==
 <StructureSection load='2k0q' size='340' side='right' caption='[[2k0q]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2k0q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cupriavidus_metallidurans Cupriavidus metallidurans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K0Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K0Q FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">copK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119219 Cupriavidus metallidurans])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">copK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119219 CUPRIAVIDUS METALLIDURANS])</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=2k0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k0q OCA], [http://pdbe.org/2k0q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k0q RCSB], [http://www.ebi.ac.uk/pdbsum/2k0q PDBsum]</span></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=2k0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k0q OCA], [http://pdbe.org/2k0q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k0q RCSB], [http://www.ebi.ac.uk/pdbsum/2k0q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k0q ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k0/2k0q_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k0/2k0q_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 40: / Line 41: @@
 [[Category: Vallaeys, T]]
 [[Category: Wattiez, R]]
+[[Category: Copper]]
 [[Category: Heavy metal resistance]]
 [[Category: Metal binding protein]]
 [[Category: Open barrel]]
 [[Category: Plasmid-encoded]]

2k0q

From Proteopedia

Revision as of 10:24, 18 July 2018

Solution structure of CopK, a periplasmic protein involved in copper resistance in Cupriavidus metallidurans CH34

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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