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The isolated Cys(2)His(2) site in EC metallothionein mediates metal-specific protein folding
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Leszczyszyn, Oksana I., White, Craig Roy J. and Blindauer, Claudia A.. (2010) The isolated Cys(2)His(2) site in EC metallothionein mediates metal-specific protein folding. Molecular BioSystems, Vol.6 (No.9). pp. 1592-1603. ISSN 1742-206X
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Official URL: http://dx.doi.org/10.1039/c002348e
Abstract
The selectivity of proteins involved in metal ion homeostasis is an important part of the puzzle to understand how cells allocate the correct metal ions to the correct proteins. Due to their similar ligand-binding properties, and their frequent co-existence in soils, essential zinc and toxic cadmium are a particularly challenging couple. Thus, minimisation of competition of Cd2+ for Zn2+ sites is of crucial importance for organisms that are in direct contact with soil. Amongst these, plants have an especially critical role, due to their importance for nutrition and energy. We have studied an embryo-specific, zinc-binding metallothionein (EC) from wheat by nuclear magnetic resonance, electrospray mass spectrometry, site-directed mutagenesis, and molecular modelling. Wheat EC exploits differences in affinities of Cys(4) and Cys(2)His(2) sites for Cd2+ and Zn2+ to achieve metal-selective protein folding. We propose that this may constitute a novel mechanism to discriminate between essential Zn2+ and toxic Cd2+.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QD Chemistry Q Science > QP Physiology |
| Divisions: | Faculty of Science > Chemistry |
| Library of Congress Subject Headings (LCSH): | Metallothionein, Zinc-finger proteins, Metal ions, Ligand binding (Biochemistry), Protein folding |
| Journal or Publication Title: | Molecular BioSystems |
| Publisher: | Royal Society of Chemistry |
| ISSN: | 1742-206X |
| Official Date: | 2010 |
| Volume: | Vol.6 |
| Number: | No.9 |
| Number of Pages: | 12 |
| Page Range: | pp. 1592-1603 |
| Identification Number: | 10.1039/c002348e |
| Status: | Peer Reviewed |
| Publication Status: | Published |
| Access rights to Published version: | Restricted or Subscription Access |
| Funder: | Royal Society (Great Britain), Engineering and Physical Sciences Research Council (EPSRC), Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC) |
| URI: | http://wrap.warwick.ac.uk/id/eprint/5362 |
Data sourced from Thomson Reuters' Web of Knowledge
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