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A Mets motif peptide found in copper transport proteins selectively binds Cu(I) with methionine-only coordination.

Publication ,  Journal Article
Jiang, J; Nadas, IA; Kim, MA; Franz, KJ
Published in: Inorganic chemistry
December 2005

Mets motifs, which refer to methionine-rich sequences found in the high-affinity copper transporter Ctr1, also appear in other proteins involved in copper trafficking and homeostasis, including other Ctrs as well as Pco and Cop proteins isolated from copper-resistant bacteria. To understand the coordination chemistry utilized by these proteins, we studied the copper binding properties of a peptide labeled Mets7-PcoC with the sequence Met-Thr-Gly-Met-Lys-Gly-Met-Ser. By comparing this sequence to a series of mutants containing noncoordinating norleucine in place of methionine, we confirm that all three methionine residues are involved in a thioether-only binding site that is selective for Cu(I). Two independent methods, one based on mass spectrometry and one based on rate differences for the copper-catalyzed oxidation of ascorbic acid, provide an effective K(D) of approximately 2.5 microM at pH 4.5 for the 1:1 complex of Mets7-PcoC with Cu(I). These results establish that a relatively simple peptide containing an MX(2)MX(2)M motif is sufficient to bind Cu(I) with an affinity that corresponds well with its proposed biological function of extracellular copper acquisition.

Duke Scholars

Published In

Inorganic chemistry

DOI

EISSN

1520-510X

ISSN

0020-1669

Publication Date

December 2005

Volume

44

Issue

26

Start / End Page

9787 / 9794

Related Subject Headings

  • Spectrometry, Mass, Electrospray Ionization
  • Peptides
  • Oxidation-Reduction
  • Oligopeptides
  • Methionine
  • Inorganic & Nuclear Chemistry
  • Copper
  • Carrier Proteins
  • Biological Transport
  • Ascorbic Acid
 

Citation

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Jiang, J., Nadas, I. A., Kim, M. A., & Franz, K. J. (2005). A Mets motif peptide found in copper transport proteins selectively binds Cu(I) with methionine-only coordination. Inorganic Chemistry, 44(26), 9787–9794. https://doi.org/10.1021/ic051180m
Jiang, Jianfeng, Istvan A. Nadas, M Alison Kim, and Katherine J. Franz. “A Mets motif peptide found in copper transport proteins selectively binds Cu(I) with methionine-only coordination.Inorganic Chemistry 44, no. 26 (December 2005): 9787–94. https://doi.org/10.1021/ic051180m.
Jiang J, Nadas IA, Kim MA, Franz KJ. A Mets motif peptide found in copper transport proteins selectively binds Cu(I) with methionine-only coordination. Inorganic chemistry. 2005 Dec;44(26):9787–94.
Jiang, Jianfeng, et al. “A Mets motif peptide found in copper transport proteins selectively binds Cu(I) with methionine-only coordination.Inorganic Chemistry, vol. 44, no. 26, Dec. 2005, pp. 9787–94. Epmc, doi:10.1021/ic051180m.
Jiang J, Nadas IA, Kim MA, Franz KJ. A Mets motif peptide found in copper transport proteins selectively binds Cu(I) with methionine-only coordination. Inorganic chemistry. 2005 Dec;44(26):9787–9794.
Journal cover image

Published In

Inorganic chemistry

DOI

EISSN

1520-510X

ISSN

0020-1669

Publication Date

December 2005

Volume

44

Issue

26

Start / End Page

9787 / 9794

Related Subject Headings

  • Spectrometry, Mass, Electrospray Ionization
  • Peptides
  • Oxidation-Reduction
  • Oligopeptides
  • Methionine
  • Inorganic & Nuclear Chemistry
  • Copper
  • Carrier Proteins
  • Biological Transport
  • Ascorbic Acid