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Model Peptide Studies Reveal a Mixed Histidine-Methionine Cu(I) Binding Site at the N-Terminus of Human Copper Transporter 1.

Publication ,  Journal Article
Pushie, MJ; Shaw, K; Franz, KJ; Shearer, J; Haas, KL
Published in: Inorganic chemistry
September 2015

Copper is a vital metal cofactor in enzymes that are essential to myriad biological processes. Cellular acquisition of copper is primarily accomplished through the Ctr family of plasma membrane copper transport proteins. Model peptide studies indicate that the human Ctr1 N-terminus binds to Cu(II) with high affinity through an amino terminal Cu(II), Ni(II) (ATCUN) binding site. Unlike typical ATCUN-type peptides, the Ctr1 peptide facilitates the ascorbate-dependent reduction of Cu(II) bound in its ATCUN site by virtue of an adjacent HH (bis-His) sequence in the peptide. It is likely that the Cu(I) coordination environment influences the redox behavior of Cu bound to this peptide; however, the identity and coordination geometry of the Cu(I) site has not been elucidated from previous work. Here, we show data from NMR, XAS, and structural modeling that sheds light on the identity of the Cu(I) binding site of a Ctr1 model peptide. The Cu(I) site includes the same bis-His site identified in previous work to facilitate ascorbate-dependent Cu(II) reduction. The data presented here are consistent with a rational mechanism by which Ctr1 provides coordination environments that facilitate Cu(II) reduction prior to Cu(I) transport.

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Published In

Inorganic chemistry

DOI

EISSN

1520-510X

ISSN

0020-1669

Publication Date

September 2015

Volume

54

Issue

17

Start / End Page

8544 / 8551

Related Subject Headings

  • X-Ray Absorption Spectroscopy
  • Quantum Theory
  • Peptides
  • Molecular Structure
  • Models, Molecular
  • Methionine
  • Inorganic & Nuclear Chemistry
  • Humans
  • Histidine
  • Copper Transporter 1
 

Citation

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Pushie, M. J., Shaw, K., Franz, K. J., Shearer, J., & Haas, K. L. (2015). Model Peptide Studies Reveal a Mixed Histidine-Methionine Cu(I) Binding Site at the N-Terminus of Human Copper Transporter 1. Inorganic Chemistry, 54(17), 8544–8551. https://doi.org/10.1021/acs.inorgchem.5b01162
Pushie, M Jake, Katharine Shaw, Katherine J. Franz, Jason Shearer, and Kathryn L. Haas. “Model Peptide Studies Reveal a Mixed Histidine-Methionine Cu(I) Binding Site at the N-Terminus of Human Copper Transporter 1.Inorganic Chemistry 54, no. 17 (September 2015): 8544–51. https://doi.org/10.1021/acs.inorgchem.5b01162.
Pushie MJ, Shaw K, Franz KJ, Shearer J, Haas KL. Model Peptide Studies Reveal a Mixed Histidine-Methionine Cu(I) Binding Site at the N-Terminus of Human Copper Transporter 1. Inorganic chemistry. 2015 Sep;54(17):8544–51.
Pushie, M. Jake, et al. “Model Peptide Studies Reveal a Mixed Histidine-Methionine Cu(I) Binding Site at the N-Terminus of Human Copper Transporter 1.Inorganic Chemistry, vol. 54, no. 17, Sept. 2015, pp. 8544–51. Epmc, doi:10.1021/acs.inorgchem.5b01162.
Pushie MJ, Shaw K, Franz KJ, Shearer J, Haas KL. Model Peptide Studies Reveal a Mixed Histidine-Methionine Cu(I) Binding Site at the N-Terminus of Human Copper Transporter 1. Inorganic chemistry. 2015 Sep;54(17):8544–8551.
Journal cover image

Published In

Inorganic chemistry

DOI

EISSN

1520-510X

ISSN

0020-1669

Publication Date

September 2015

Volume

54

Issue

17

Start / End Page

8544 / 8551

Related Subject Headings

  • X-Ray Absorption Spectroscopy
  • Quantum Theory
  • Peptides
  • Molecular Structure
  • Models, Molecular
  • Methionine
  • Inorganic & Nuclear Chemistry
  • Humans
  • Histidine
  • Copper Transporter 1