1RK7

Solution structure of apo Cu,Zn Superoxide Dismutase: role of metal ions in protein folding

1RK7 の概要

• エントリーDOI: 10.2210/pdb1rk7/pdb
• 関連するPDBエントリー: 1ba9
• NMR情報: BMRB: 4202
• 分子名称: Superoxide dismutase [Cu-Zn] (1 entity in total)
• 機能のキーワード: apo form of monomeric mutant of cu, zn sod; solution structure, q133m2sod, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P00441
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15832.45

構造登録者

Banci, L.,Bertini, I.,Cramaro, F.,Del Conte, R.,Viezzoli, M.S. (登録日: 2003-11-21, 公開日: 2003-12-02, 最終更新日: 2024-11-13)

主引用文献

Banci, L.,Bertini, I.,Cramaro, F.,Del Conte, R.,Viezzoli, M.S.
Solution structure of Apo Cu,Zn Superoxide Dismutase: Role of Metal Ions in Protein Folding
Biochemistry, 42:9543-9553, 2003

PubMed Abstract: The solution structure of the demetalated copper, zinc superoxide dismutase is obtained for the monomeric Glu133Gln/Phe50Glu/Gly51Glu mutant through NMR spectroscopy. The demetalated protein still has a well-defined tertiary structure; however, two beta-strands containing two copper ligands (His46 and His48, beta4) and one zinc ligand (Asp83, beta5) are shortened, and the sheet formed by these strands and strands beta7 and beta8 moves away from the other strands of the beta-barrel to form an open clam with respect to a closed conformation in the holoprotein. Furthermore, loop IV which contains three zinc ligands (His63, His71, and His80) and loop VII which contributes to the definition of the active cavity channel are severely disordered, and experience extensive mobility as it results from thorough (15)N relaxation measurements. These structural and mobility data, if compared with those of the copper-depleted protein and holoprotein, point out the role of each metal ion in the protein folding, leading to the final tertiary structure of the holoprotein, and provide hints for the mechanisms of metal delivery by metal chaperones.

PubMed: 12911296
DOI: 10.1021/bi034324m

実験手法

SOLUTION NMR