Structural highlights
Function
EC1_WHEAT Binds 5 molecules of zinc. May have a role in Zn(2+) homeostasis during embryogenesis.
Publication Abstract from PubMed
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.
Solution Structure of the Circular gamma-Domain Analog from the Wheat Metallothionein Ec-1.,Tarasava K, Johannsen S, Freisinger E Molecules. 2013 Nov 21;18(11):14414-29. doi: 10.3390/molecules181114414. PMID:24284492[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tarasava K, Johannsen S, Freisinger E. Solution Structure of the Circular gamma-Domain Analog from the Wheat Metallothionein Ec-1. Molecules. 2013 Nov 21;18(11):14414-29. doi: 10.3390/molecules181114414. PMID:24284492 doi:http://dx.doi.org/10.3390/molecules181114414
