2RLI

Solution structure of Cu(I) human Sco2

2RLI の概要

• エントリーDOI: 10.2210/pdb2rli/pdb
• 分子名称: SCO2 protein homolog, mitochondrial, COPPER (I) ION (2 entities in total)
• 機能のキーワード: copper protein, thioredoxin fold, metal transport, structural genomics, spine2-complexes, structural proteomics in europe, spine, structural proteomics in europe 2, spine-2
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion: O43819
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19556.37

構造登録者

Banci, L.,Bertini, I.,Ciofi-baffoni, S.,Gerothanassis, I.P.,Leontari, I.,Martinelli, M.,Wang, S.,Structural Proteomics in Europe (SPINE),Structural Proteomics in Europe 2 (SPINE-2) (登録日: 2007-07-11, 公開日: 2007-08-28, 最終更新日: 2024-05-29)

主引用文献

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Gerothanassis, I.P.,Leontari, I.,Martinelli, M.,Wang, S.
A Structural Characterization of Human SCO2
Structure, 15:1132-1140, 2007

PubMed Abstract: Human Sco2 is a mitochondrial membrane-bound protein involved in copper supply for the assembly of cytochrome c oxidase in eukaryotes. Its precise action is not yet understood. We report here a structural and dynamic characterization by NMR of the apo and copper(I) forms of the soluble fragment. The structural and metal binding features of human Cu(I)Sco2 are similar to the more often studied Sco1 homolog, although the dynamic properties and the conformational disorder are quite different when the apo forms and the copper(I)-loaded forms of the two proteins are compared separately. Such differences are accounted for in terms of the different physicochemical properties in strategic protein locations. The misfunction of the known pathogenic mutations is discussed on the basis of the obtained structure.

PubMed: 17850752
DOI: 10.1016/j.str.2007.07.011

実験手法

SOLUTION NMR