Issue 22, 2011
From the journal:

Chemical Communications

NMR characterization of a Cu(i)-bound peptide model of copper metallochaperones: Insights on the role of methionine†

Michal S. Shoshan,a   Deborah E. Shalev,b   Wencke Adriaens,c   Maarten Merkx,c   Tilman M. Hackengd  and  Edit Y. Tshuva*a  

* Corresponding authors

a Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel
E-mail: tshuva@chem.ch.huji.ac.il
Fax: +972 2 658 4282
Tel: +972 2 658 6084

b Wolfson Centre for Applied Structural Biology, The Hebrew University of Jerusalem, Jerusalem, Israel

c Laboratory of Chemical Biology, Department of Biomedical Engineering, Eindhoven University of Technology, The Netherlands

d Department of Biochemistry, Maastricht University Medical Center, The Netherlands

Abstract

The first NMR structure of a Cu(I)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH ∼3.0 and ∼6.8 Cu(I) binds through one Cys and the Met rather than the two Cys residues, differently than at pH ∼8.5. This suggests a possible role of Met in metal transport.

Graphical abstract: NMR characterization of a Cu(i)-bound peptide model of copper metallochaperones: Insights on the role of methionine

About
Cited by
Related
Download options Please wait...

Supplementary files

Article information

DOI
https://doi.org/10.1039/C1CC11600B
Article type
Communication
Submitted
20 Mar 2011
Accepted
18 Apr 2011
First published
09 May 2011

Chem. Commun., 2011,47, 6407-6409

Permissions

Request permissions

NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: Insights on the role of methionine

M. S. Shoshan, D. E. Shalev, W. Adriaens, M. Merkx, T. M. Hackeng and E. Y. Tshuva, Chem. Commun., 2011, 47, 6407 DOI: 10.1039/C1CC11600B

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements