---
_id: '8481'
abstract:
- lang: eng
  text: '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-β fold formed of two β-sheets
    in perpendicular orientation with an unstructured C-terminal tail. The dimer interface
    is formed by the surface of the C-terminal β-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 β-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 β-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-β fold and the methionine-rich Cu(I)-binding site.'
article_processing_charge: No
article_type: original
author:
- first_name: Beate
  full_name: Bersch, Beate
  last_name: Bersch
- first_name: Adrien
  full_name: Favier, Adrien
  last_name: Favier
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Sébastien
  full_name: van Aelst, Sébastien
  last_name: van Aelst
- first_name: Tatiana
  full_name: Vallaeys, Tatiana
  last_name: Vallaeys
- first_name: Jacques
  full_name: Covès, Jacques
  last_name: Covès
- first_name: Max
  full_name: Mergeay, Max
  last_name: Mergeay
- first_name: Ruddy
  full_name: Wattiez, Ruddy
  last_name: Wattiez
citation:
  ama: Bersch B, Favier A, Schanda P, et al. Molecular structure and metal-binding
    properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans
    CH34 during copper challenge. <i>Journal of Molecular Biology</i>. 2008;380(2):386-403.
    doi:<a href="https://doi.org/10.1016/j.jmb.2008.05.017">10.1016/j.jmb.2008.05.017</a>
  apa: Bersch, B., Favier, A., Schanda, P., van Aelst, S., Vallaeys, T., Covès, J.,
    … Wattiez, R. (2008). Molecular structure and metal-binding properties of the
    periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper
    challenge. <i>Journal of Molecular Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.jmb.2008.05.017">https://doi.org/10.1016/j.jmb.2008.05.017</a>
  chicago: Bersch, Beate, Adrien Favier, Paul Schanda, Sébastien van Aelst, Tatiana
    Vallaeys, Jacques Covès, Max Mergeay, and Ruddy Wattiez. “Molecular Structure
    and Metal-Binding Properties of the Periplasmic CopK Protein Expressed in Cupriavidus
    Metallidurans CH34 during Copper Challenge.” <i>Journal of Molecular Biology</i>.
    Elsevier, 2008. <a href="https://doi.org/10.1016/j.jmb.2008.05.017">https://doi.org/10.1016/j.jmb.2008.05.017</a>.
  ieee: B. Bersch <i>et al.</i>, “Molecular structure and metal-binding properties
    of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during
    copper challenge,” <i>Journal of Molecular Biology</i>, vol. 380, no. 2. Elsevier,
    pp. 386–403, 2008.
  ista: Bersch B, Favier A, Schanda P, van Aelst S, Vallaeys T, Covès J, Mergeay M,
    Wattiez R. 2008. Molecular structure and metal-binding properties of the periplasmic
    CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge.
    Journal of Molecular Biology. 380(2), 386–403.
  mla: Bersch, Beate, et al. “Molecular Structure and Metal-Binding Properties of
    the Periplasmic CopK Protein Expressed in Cupriavidus Metallidurans CH34 during
    Copper Challenge.” <i>Journal of Molecular Biology</i>, vol. 380, no. 2, Elsevier,
    2008, pp. 386–403, doi:<a href="https://doi.org/10.1016/j.jmb.2008.05.017">10.1016/j.jmb.2008.05.017</a>.
  short: B. Bersch, A. Favier, P. Schanda, S. van Aelst, T. Vallaeys, J. Covès, M.
    Mergeay, R. Wattiez, Journal of Molecular Biology 380 (2008) 386–403.
date_created: 2020-09-18T10:12:37Z
date_published: 2008-07-04T00:00:00Z
date_updated: 2021-01-12T08:19:34Z
day: '04'
doi: 10.1016/j.jmb.2008.05.017
extern: '1'
intvolume: '       380'
issue: '2'
keyword:
- Molecular Biology
language:
- iso: eng
month: '07'
oa_version: None
page: 386-403
publication: Journal of Molecular Biology
publication_identifier:
  issn:
  - 0022-2836
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Molecular structure and metal-binding properties of the periplasmic CopK protein
  expressed in Cupriavidus metallidurans CH34 during copper challenge
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 380
year: '2008'
...