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Molecules 2013, 18(11), 14414-14429; doi:10.3390/molecules181114414

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

Institute of Inorganic Chemistry, University of Zurich, Winterthurerstrasse 190, Zurich CH-8057, Switzerland
These authors contributed equally to this work.
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Received: 16 October 2013 / Revised: 6 November 2013 / Accepted: 19 November 2013 / Published: 21 November 2013
(This article belongs to the Special Issue NMR of Proteins and Small Biomolecules)
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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 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. View Full-Text
Keywords: plant metallothioneins; metal-thiolate cluster; backbone cyclization; flexibility reduction; NMR spectroscopy plant metallothioneins; metal-thiolate cluster; backbone cyclization; flexibility reduction; NMR spectroscopy
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MDPI and ACS Style

Tarasava, K.; Johannsen, S.; Freisinger, E. Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-1. Molecules 2013, 18, 14414-14429.

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