Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-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 g-Ec-1 domain of the wheat MT Ec-1 retains its ability to coordinate two Zn(II) or Cd(II) ion...

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Main Authors: Katsiaryna Tarasava, Silke Johannsen, Eva Freisinger
Format: Article
Language:English
Published: MDPI AG 2013-11-01
Series:Molecules
Subjects:
Online Access:http://www.mdpi.com/1420-3049/18/11/14414
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spelling doaj-c593beb69e884e84a0cb68a1a27005ef2020-11-24T22:57:45ZengMDPI AGMolecules1420-30492013-11-011811144141442910.3390/molecules181114414molecules181114414Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-1Katsiaryna Tarasava0Silke Johannsen1Eva Freisinger2Institute of Inorganic Chemistry, University of Zurich, Winterthurerstrasse 190, Zurich CH-8057, SwitzerlandInstitute of Inorganic Chemistry, University of Zurich, Winterthurerstrasse 190, Zurich CH-8057, SwitzerlandInstitute of Inorganic Chemistry, University of Zurich, Winterthurerstrasse 190, Zurich CH-8057, SwitzerlandThe 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 g-Ec-1 domain of the wheat MT Ec-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.http://www.mdpi.com/1420-3049/18/11/14414plant metallothioneinsmetal-thiolate clusterbackbone cyclizationflexibility reductionNMR spectroscopy
collection DOAJ
language English
format Article
sources DOAJ
author Katsiaryna Tarasava
Silke Johannsen
Eva Freisinger
spellingShingle Katsiaryna Tarasava
Silke Johannsen
Eva Freisinger
Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-1
Molecules
plant metallothioneins
metal-thiolate cluster
backbone cyclization
flexibility reduction
NMR spectroscopy
author_facet Katsiaryna Tarasava
Silke Johannsen
Eva Freisinger
author_sort Katsiaryna Tarasava
title Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-1
title_short Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-1
title_full Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-1
title_fullStr Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-1
title_full_unstemmed Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-1
title_sort solution structure of the circular γ-domain analog from the wheat metallothionein ec-1
publisher MDPI AG
series Molecules
issn 1420-3049
publishDate 2013-11-01
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 g-Ec-1 domain of the wheat MT Ec-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.
topic plant metallothioneins
metal-thiolate cluster
backbone cyclization
flexibility reduction
NMR spectroscopy
url http://www.mdpi.com/1420-3049/18/11/14414
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AT silkejohannsen solutionstructureofthecirculargdomainanalogfromthewheatmetallothioneinec1
AT evafreisinger solutionstructureofthecirculargdomainanalogfromthewheatmetallothioneinec1
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