1ON4

Solution structure of soluble domain of Sco1 from Bacillus Subtilis

1ON4 の概要

• エントリーDOI: 10.2210/pdb1on4/pdb
• NMR情報: BMRB: 5742
• 分子名称: Sco1 (1 entity in total)
• 機能のキーワード: cox assembly protein, copper protein, sco1 from b. subtilis, thioredoxin-like fold, ypmq, structural proteomics in europe, spine, structural genomics, metal binding protein
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cell membrane; Lipid-anchor; Cytoplasmic side: P54178
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19856.35

構造登録者

Balatri, E.,Banci, L.,Bertini, I.,Cantini, F.,Ciofi-Baffoni, S.,Structural Proteomics in Europe (SPINE) (登録日: 2003-02-27, 公開日: 2003-11-11, 最終更新日: 2024-05-29)

主引用文献

Balatri, E.,Banci, L.,Bertini, I.,Cantini, F.,Ciofi-Baffoni, S.
Solution Structure of Sco1: A Thioredoxin-like Protein Involved in Cytochrome c Oxidase Assembly
STRUCTURE, 11:1431-1433, 2003

PubMed Abstract: Sco1, a protein required for the proper assembly of cytochrome c oxidase, has a soluble domain anchored to the cytoplasmic membrane through a single transmembrane segment. The solution structure of the soluble part of apoSco1 from Bacillus subtilis has been solved by NMR and the internal mobility characterized. Its fold places Sco1 in a distinct subgroup of the functionally unrelated thioredoxin proteins. In vitro Sco1 binds copper(I) through a CXXXCP motif and possibly His 135 and copper(II) in two different species, thus suggesting that copper(II) is adventitious more than physiological. The Sco1 structure represents the first structure of this class of proteins, present in a variety of eukaryotic and bacterial organisms, and elucidates a link between copper trafficking proteins and thioredoxins. The availability of the structure has allowed us to model the homologs Sco1 and Sco2 from S. cerevisiae and to discuss the physiological role of the Sco family.

PubMed: 14604533
DOI: 10.1016/j.str.2003.10.004

実験手法

SOLUTION NMR