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

Overview

Journal Molecules

Publisher MDPI

Specialty Biology

Date 2013 Nov 29

PMID 24284492

Citations 2

Authors

Katsiaryna Tarasava

Silke Johannsen

Eva Freisinger

Affiliations

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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 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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