6N5U
Crystal structure of Arabidopsis thaliana ScoI with copper bound
6N5U の概要
| エントリーDOI | 10.2210/pdb6n5u/pdb |
| 分子名称 | Protein SCO1 homolog 1, mitochondrial, COPPER (I) ION (3 entities in total) |
| 機能のキーワード | thioredoxin fold, metal ion, reduced form, metallochaperone, hcc1, metal binding protein |
| 由来する生物種 | Arabidopsis thaliana (Mouse-ear cress) |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 58457.26 |
| 構造登録者 | Lisa, M.N.,Giannini, E.,Llases, M.E.,Alzari, P.M.,Vila, A.J. (登録日: 2018-11-22, 公開日: 2019-07-24, 最終更新日: 2023-10-11) |
| 主引用文献 | Llases, M.E.,Lisa, M.N.,Morgada, M.N.,Giannini, E.,Alzari, P.M.,Vila, A.J. Arabidopsis thaliana Hcc1 is a Sco-like metallochaperone for CuAassembly in Cytochrome c Oxidase. Febs J., 287:749-762, 2020 Cited by PubMed Abstract: The assembly of the Cu site in Cytochrome c Oxidase (COX) is a critical step for aerobic respiration in COX-dependent organisms. Several gene products have been associated with the assembly of this copper site, the most conserved of them belonging to the Sco family of proteins, which have been shown to perform different roles in different organisms. Plants express two orthologs of Sco proteins: Hcc1 and Hcc2. Hcc1 is known to be essential for plant development and for COX maturation, but its precise function has not been addressed until now. Here, we report the biochemical, structural and functional characterization of Arabidopsis thaliana Hcc1 protein (here renamed Sco1). We solved the crystal structure of the Cu -bound soluble domain of this protein, revealing a tri coordinated environment involving a CxxxCx H motif. We show that AtSco1 is able to work as a copper metallochaperone, inserting two Cu ions into the Cu site in a model of CoxII. We also show that AtSco1 does not act as a thiol-disulfide oxido-reductase. Overall, this information sheds new light on the biochemistry of Sco proteins, highlighting the diversity of functions among them despite their high structural similarities. DATABASE: PDB entry 6N5U (Crystal structure of Arabidopsis thaliana ScoI with copper bound). PubMed: 31348612DOI: 10.1111/febs.15016 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.66 Å) |
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