Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein E(c)-1

The first cyclic analog of a metallothionein (MT) was prepared and analyzed by UV and (magnetic) circular dichroism spectroscopy, ESI-MS as well as NMR spectroscopy. Results reveal that the evaluated cyclic γ-E(c)-1 domain of the wheat MT E(c)-1 retains its ability to coordinate two Zn(II) or Cd(II)...

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Autores principales: Tarasava, Katsiaryna, Johannsen, Silke, Freisinger, Eva
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6269658/
https://www.ncbi.nlm.nih.gov/pubmed/24284492
http://dx.doi.org/10.3390/molecules181114414
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author Tarasava, Katsiaryna
Johannsen, Silke
Freisinger, Eva
author_facet Tarasava, Katsiaryna
Johannsen, Silke
Freisinger, Eva
author_sort Tarasava, Katsiaryna
collection PubMed
description The first cyclic analog of a metallothionein (MT) was prepared and analyzed by UV and (magnetic) circular dichroism spectroscopy, ESI-MS as well as NMR spectroscopy. Results reveal that the evaluated cyclic γ-E(c)-1 domain of the wheat MT E(c)-1 retains its ability to coordinate two Zn(II) or Cd(II) ions and adopts a three-dimensional structure that is highly similar to the one of the linear wild-type form. However, the reduced flexibility of the protein backbone facilitates structure solution significantly and results in a certain stabilization of metal binding to the protein.
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spelling pubmed-62696582018-12-20 Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein E(c)-1 Tarasava, Katsiaryna Johannsen, Silke Freisinger, Eva Molecules Article The first cyclic analog of a metallothionein (MT) was prepared and analyzed by UV and (magnetic) circular dichroism spectroscopy, ESI-MS as well as NMR spectroscopy. Results reveal that the evaluated cyclic γ-E(c)-1 domain of the wheat MT E(c)-1 retains its ability to coordinate two Zn(II) or Cd(II) ions and adopts a three-dimensional structure that is highly similar to the one of the linear wild-type form. However, the reduced flexibility of the protein backbone facilitates structure solution significantly and results in a certain stabilization of metal binding to the protein. MDPI 2013-11-21 /pmc/articles/PMC6269658/ /pubmed/24284492 http://dx.doi.org/10.3390/molecules181114414 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Tarasava, Katsiaryna
Johannsen, Silke
Freisinger, Eva
Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein E(c)-1
title Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein E(c)-1
title_full Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein E(c)-1
title_fullStr Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein E(c)-1
title_full_unstemmed Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein E(c)-1
title_short Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein E(c)-1
title_sort solution structure of the circular γ-domain analog from the wheat metallothionein e(c)-1
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6269658/
https://www.ncbi.nlm.nih.gov/pubmed/24284492
http://dx.doi.org/10.3390/molecules181114414
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AT johannsensilke solutionstructureofthecirculargdomainanalogfromthewheatmetallothioneinec1
AT freisingereva solutionstructureofthecirculargdomainanalogfromthewheatmetallothioneinec1

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