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6N5U

Crystal structure of Arabidopsis thaliana ScoI with copper bound

6N5U の概要
エントリーDOI10.2210/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: 31348612
DOI: 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)
構造検証レポート
Validation report summary of 6n5u
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-29に公開中

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