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Protein and metal cluster structure of the wheat metallothionein domain gamma-Ec-1: the second part of the puzzle


Loebus, J; Peroza, E; Blüthgen, N; Fox, T; Meyer-Klaucke, W; Zerbe, O; Freisinger, E (2011). Protein and metal cluster structure of the wheat metallothionein domain gamma-Ec-1: the second part of the puzzle. Journal of Biological Inorganic Chemistry, 16(5):683-694.

Abstract

Metallothioneins (MTs) are small cysteine-rich proteins coordinating various transition metal ions, including ZnII, CdII, and CuI. MTs are ubiquitously present in all phyla, indicating a successful molecular concept for metal ion binding in all organisms. The plant MT Ec-1 from Triticum aestivum, common bread wheat, is a ZnII- binding protein that comprises two domains and binds up to six metal ions. The structure of the C-terminal four metal ion binding beta-E domain was recently described. Here we present the structure of the N-terminal second domain, gama-Ec-1, determined by NMR spectroscopy. The gamma-Ec-1 domain enfolds an MIICys cluster and was characterized as part of the full-length Zn6Ec-1 protein as well as in the
form of the separately expressed domain, both in the ZnII-containing isoform and the CdII-containing isoform. Extended X-ray absorption fine structure analysis of Zn2g- Ec-1 clearly shows the presence of a ZnS4 coordination sphere with average Zn–S distances of 2.33 A ̊. 113Cd NMR experiments were used to identify the MII-Cys connectivity pattern, and revealed two putative metal cluster confor- mations. In addition, the general metal ion coordination abilities of g-Ec-1 were probed with CdII binding experi- ments as well as by pH titrations of the ZnII and CdII forms, the latter suggesting an interaction of the c domain and the bE domain within the full-length protein.

Metallothioneins (MTs) are small cysteine-rich proteins coordinating various transition metal ions, including ZnII, CdII, and CuI. MTs are ubiquitously present in all phyla, indicating a successful molecular concept for metal ion binding in all organisms. The plant MT Ec-1 from Triticum aestivum, common bread wheat, is a ZnII- binding protein that comprises two domains and binds up to six metal ions. The structure of the C-terminal four metal ion binding beta-E domain was recently described. Here we present the structure of the N-terminal second domain, gama-Ec-1, determined by NMR spectroscopy. The gamma-Ec-1 domain enfolds an MIICys cluster and was characterized as part of the full-length Zn6Ec-1 protein as well as in the
form of the separately expressed domain, both in the ZnII-containing isoform and the CdII-containing isoform. Extended X-ray absorption fine structure analysis of Zn2g- Ec-1 clearly shows the presence of a ZnS4 coordination sphere with average Zn–S distances of 2.33 A ̊. 113Cd NMR experiments were used to identify the MII-Cys connectivity pattern, and revealed two putative metal cluster confor- mations. In addition, the general metal ion coordination abilities of g-Ec-1 were probed with CdII binding experi- ments as well as by pH titrations of the ZnII and CdII forms, the latter suggesting an interaction of the c domain and the bE domain within the full-length protein.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Uncontrolled Keywords:NMR plant metallothionein structural biology
Language:English
Date:2011
Deposited On:28 Oct 2011 12:31
Last Modified:05 Apr 2016 15:03
Publisher:Springer
ISSN:0949-8257
Publisher DOI:https://doi.org/10.1007/s00775-011-0770-2
PubMed ID:21437709
Permanent URL: https://doi.org/10.5167/uzh-50365

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