title: Solution structure of the circular γ-domain analog from the wheat metallothionein E(c)-1.
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.
authors.affiliation: Institute of Inorganic Chemistry, University of Zurich, Winterthurerstrasse 190, Zurich CH-8057, Switzerland. freisinger@aci.uzh.ch.
authors.forename: Katsiaryna
authors.initials: K
authors.lastname: Tarasava
authors.forename: Silke
authors.initials: S
authors.lastname: Johannsen
authors.forename: Eva
authors.initials: E
authors.lastname: Freisinger
mesh_terms: D008668:Metallothionein / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D014908:Triticum / Q000737:chemistry*
chemical_list: D008668:Metallothionein