This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1cpz

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

COPPER CHAPERONE OF ENTEROCOCCUS HIRAE (APO-FORM)

Structural highlights

1cpz is a 1 chain structure with sequence from Enterococcus hirae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

COPZ_ENTHA Acts as a copper chaperone by delivering 2 Cu(+) ions to CopY Zn(2+)-bound form. This transfer results in displacement of zinc and dissociation of CopY from the promoter, allowing transcription of the copYZAB operon.^[1] ^[2] ^[3]

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

A recently discovered family of proteins that function as copper chaperones route copper to proteins that either require it for their function or are involved in its transport. In Enterococcus hirae the copper chaperone function is performed by the 8-kDa protein CopZ. This paper describes the NMR structure of apo-CopZ, obtained using uniformly (15)N-labeled CopZ overexpressed in Escherichia coli and NMR studies of the impact of Cu(I) binding on the CopZ structure. The protein has a betaalphabetabetaalphabeta fold, where the four beta-strands form an antiparallel twisted beta-sheet, and the two helices are located on the same side of the beta-sheet. A sequence motif GMXCXXC in the loop between the first beta-strand and the first alpha-helix contains the primary ligands, which bind copper(I). Binding of copper(I) caused major structural changes in this molecular region, as manifested by the fact that most NMR signals of the loop and the N-terminal part of the first helix were broadened beyond detection. This effect was strictly localized, because the remainder of the apo-CopZ structure was maintained after addition of Cu(I). NMR relaxation data showed a decreased correlation time of overall molecular tumbling for Cu(I)-CopZ when compared with apo-CopZ, indicating aggregation of Cu(I)-CopZ. The structure of CopZ is the first three-dimensional structure of a cupro-protein for which the metal ion is an exchangeable substrate rather than an integral part of the structure. Implications of the present structural work for the in vivo function of CopZ are discussed, whereby it is of special interest that the distribution of charged residues on the CopZ surface is highly uneven and suggests preferred recognition sites for other proteins that might be involved in copper transfer.

NMR structure and metal interactions of the CopZ copper chaperone.,Wimmer R, Herrmann T, Solioz M, Wuthrich K J Biol Chem. 1999 Aug 6;274(32):22597-603. PMID:10428839^[4]

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

References

↑ Cobine P, Wickramasinghe WA, Harrison MD, Weber T, Solioz M, Dameron CT. The Enterococcus hirae copper chaperone CopZ delivers copper(I) to the CopY repressor. FEBS Lett. 1999 Feb 19;445(1):27-30. PMID:10069368
↑ Cobine PA, George GN, Jones CE, Wickramasinghe WA, Solioz M, Dameron CT. Copper transfer from the Cu(I) chaperone, CopZ, to the repressor, Zn(II)CopY: metal coordination environments and protein interactions. Biochemistry. 2002 May 7;41(18):5822-9. PMID:11980486
↑ Odermatt A, Solioz M. Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPases of Enterococcus hirae. J Biol Chem. 1995 Mar 3;270(9):4349-54. PMID:7876197
↑ Wimmer R, Herrmann T, Solioz M, Wuthrich K. NMR structure and metal interactions of the CopZ copper chaperone. J Biol Chem. 1999 Aug 6;274(32):22597-603. PMID:10428839

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/1cpz"

@@ Line 1: / Line 1: @@
 ==COPPER CHAPERONE OF ENTEROCOCCUS HIRAE (APO-FORM)==
-<StructureSection load='1cpz' size='340' side='right'caption='[[1cpz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1cpz' size='340' side='right'caption='[[1cpz]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1cpz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CPZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CPZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1cpz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_hirae Enterococcus hirae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CPZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CPZ FirstGlance]. <br>
-</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=1cpz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cpz OCA], [https://pdbe.org/1cpz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cpz RCSB], [https://www.ebi.ac.uk/pdbsum/1cpz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cpz ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1cpz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cpz OCA], [https://pdbe.org/1cpz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cpz RCSB], [https://www.ebi.ac.uk/pdbsum/1cpz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cpz ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/COPZ_ENTHA COPZ_ENTHA]] Acts as a copper chaperone by delivering 2 Cu(+) ions to CopY Zn(2+)-bound form. This transfer results in displacement of zinc and dissociation of CopY from the promoter, allowing transcription of the copYZAB operon.<ref>PMID:10069368</ref> <ref>PMID:11980486</ref> <ref>PMID:7876197</ref>
+[https://www.uniprot.org/uniprot/COPZ_ENTHA COPZ_ENTHA] Acts as a copper chaperone by delivering 2 Cu(+) ions to CopY Zn(2+)-bound form. This transfer results in displacement of zinc and dissociation of CopY from the promoter, allowing transcription of the copYZAB operon.<ref>PMID:10069368</ref> <ref>PMID:11980486</ref> <ref>PMID:7876197</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
+[[Category: Enterococcus hirae]]
 [[Category: Large Structures]]
-[[Category: Herrmann, T]]
+[[Category: Herrmann T]]
-[[Category: Solioz, M]]
+[[Category: Solioz M]]
-[[Category: Wimmer, R]]
+[[Category: Wimmer R]]
-[[Category: Wuethrich, K]]
+[[Category: Wuethrich K]]
-[[Category: Copper chaperone]]
-[[Category: Gene regulation]]
-[[Category: Metal transport]]

1cpz

From Proteopedia

Current revision

COPPER CHAPERONE OF ENTEROCOCCUS HIRAE (APO-FORM)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox