2L62

Protein and metal cluster structure of the wheat metallothionein domain g-Ec-1. The second part of the puzzle.

2L62 の概要

• エントリーDOI: 10.2210/pdb2l62/pdb
• 関連するPDBエントリー: 2L62
• NMR情報: BMRB: 17295
• 分子名称: EC protein I/II, ZINC ION (2 entities in total)
• 機能のキーワード: metallothionein, wheat ec-1, zn binding, metal-thiolate cluster, metal binding protein
• 由来する生物種: Triticum aestivum (Canadian hard winter wheat,common wheat,wheat)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2595.62

構造登録者

Loebus, J.,Peroza, E.A.,Bluethgen, N.,Fox, T.,Meyer-Klaucke, W.,Zerbe, O.,Freisinger, E. (登録日: 2010-11-12, 公開日: 2011-05-25, 最終更新日: 2024-05-01)

主引用文献

Loebus, J.,Peroza, E.A.,Bluthgen, N.,Fox, T.,Meyer-Klaucke, W.,Zerbe, O.,Freisinger, E.
Protein and metal cluster structure of the wheat metallothionein domain gamma-E(c)-1: the second part of the puzzle.
J.Biol.Inorg.Chem., 16:683-694, 2011

PubMed 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-E(c)-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.

PubMed: 21437709
DOI: 10.1007/s00775-011-0770-2

実験手法

SOLUTION NMR