Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-1

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...

Full description

Bibliographic Details
Main Authors: Katsiaryna Tarasava, Silke Johannsen, Eva Freisinger
Format: Article
Language:English
Published: MDPI AG 2013-11-01
Series:Molecules
Subjects:
plant metallothioneins
metal-thiolate cluster
backbone cyclization
flexibility reduction
NMR spectroscopy
Online Access:http://www.mdpi.com/1420-3049/18/11/14414
Description
Summary: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.
ISSN:1420-3049

Similar Items