2L62
Protein and metal cluster structure of the wheat metallothionein domain g-Ec-1. The second part of the puzzle.
Summary for 2L62
| Entry DOI | 10.2210/pdb2l62/pdb |
| Related | 2L62 |
| NMR Information | BMRB: 17295 |
| Descriptor | EC protein I/II, ZINC ION (2 entities in total) |
| Functional Keywords | metallothionein, wheat ec-1, zn binding, metal-thiolate cluster, metal binding protein |
| Biological source | Triticum aestivum (Canadian hard winter wheat,common wheat,wheat) |
| Total number of polymer chains | 1 |
| Total formula weight | 2595.62 |
| Authors | Loebus, J.,Peroza, E.A.,Bluethgen, N.,Fox, T.,Meyer-Klaucke, W.,Zerbe, O.,Freisinger, E. (deposition date: 2010-11-12, release date: 2011-05-25, Last modification date: 2024-05-01) |
| Primary citation | 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 Cited by 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: 21437709DOI: 10.1007/s00775-011-0770-2 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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