Journal Article

PUBDB-2016-02464

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Protein and metal cluster structure of the wheat metallothionein domain $\mathrm{\gamma-E_c-1}$: the second part of the puzzle

Loebus, J. ; Peroza, E. A. ; Blüthgen, N. ; Fox, T. ; Meyer-Klaucke, W.EMBL* ; Zerbe, O. (Corresponding author) ; Freisinger, E. (Corresponding author)

2011
Springer Berlin

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Please use a persistent id in citations: doi:10.1007/s00775-011-0770-2  doi:10.3204/PUBDB-2016-02464

Abstract: Metallothioneins (MTs) are small cysteine-rich proteins coordinating various transition metal ions, including Zn$^{II}$, Cd$^{II}$, and Cu$^{I}$. MTs are ubiquitously present in all phyla, indicating a successful molecular concept for metal ion binding in all organisms. The plant MT E$_c$-1 from Triticum aestivum, common bread wheat, is a Zn$^{II}$-binding protein that comprises two domains and binds up to six metal ions. The structure of the C-terminal four metal ion binding β$_E$ domain was recently described. Here we present the structure of the N-terminal second domain, γ-Ec-1, determined by NMR spectroscopy. The γ-E$_c$-1 domain enfolds an M$_{2}^{II}$Cys$_6$ cluster and was characterized as part of the full-length Zn$_6$E$_c$-1 protein as well as in the form of the separately expressed domain, both in the Zn$^{II}$-containing isoform and the Cd$^{II}$-containing isoform. Extended X-ray absorption fine structure analysis of Zn$_2$γ-E$_c$-1 clearly shows the presence of a ZnS$_4$ coordination sphere with average Zn–S distances of 2.33 Å. $^{113}$Cd NMR experiments were used to identify the M$^{II}$-Cys connectivity pattern, and revealed two putative metal cluster conformations. In addition, the general metal ion coordination abilities of γ-E$_c$-1 were probed with Cd$^{II}$ binding experiments as well as by pH titrations of the Zn$^{II}$ and Cd$^{II}$ forms, the latter suggesting an interaction of the γ domain and the β$_E$ domain within the full-length protein.

Note: (c) SBIC

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Contributing Institute(s):

1. EMBL (EMBL)

Research Program(s):

1. 899 - ohne Topic (POF3-899) (POF3-899)

Experiment(s):

1. Facility (machine) DORIS III

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; ; BIOSIS Previews ; Current Contents - Life Sciences ; Current Contents - Physical, Chemical and Earth Sciences ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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