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Solution structure of the circular γ-domain analog from the wheat metallothionein Ec-1


Tarasava, K; Johannsen, S; Freisinger, E (2013). Solution structure of the circular γ-domain analog from the wheat metallothionein Ec-1. Molecules, 18:14414-14429.

Abstract

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.

Abstract

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.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Language:English
Date:2013
Deposited On:03 Feb 2014 15:57
Last Modified:07 Dec 2017 08:28
Publisher:MDPI Publishing
ISSN:1420-3049
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.3390/molecules181114414

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