2AF2

Solution structure of disulfide reduced and copper depleted Human Superoxide Dismutase

2AF2 の概要

• エントリーDOI: 10.2210/pdb2af2/pdb
• NMR情報: BMRB: 6821
• 分子名称: Superoxide dismutase [Cu-Zn], ZINC ION (2 entities in total)
• 機能のキーワード: human superoxide dismutase, solution structure, homodimeric protein, disulfide bond reduced, copper depleted protein, structural genomics, structural proteomics in europe, spine, 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: 2
• 化学式量合計: 31689.68

構造登録者

Banci, L.,Bertini, I.,Cantini, F.,D'Amelio, N.,Gaggelli, E.,Structural Proteomics in Europe (SPINE) (登録日: 2005-07-25, 公開日: 2005-11-15, 最終更新日: 2024-05-29)

主引用文献

Banci, L.,Bertini, I.,Cantini, F.,D'Amelio, N.,Gaggelli, E.
Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form
J.Biol.Chem., 281:2333-2337, 2006

PubMed Abstract: SOD1 has to undergo several post-translational modifications before reaching its mature form. The protein requires insertion of zinc and copper atoms, followed by the formation of a conserved S-S bond between Cys-57 and Cys-146 (human numbering), which makes the protein fully active. In this report an NMR structural investigation of the reduced SH-SH form of thermostable E,Zn-as-SOD1 (E is empty; as is C6A, C111S) is reported, characterizing the protein just before the last step leading to the mature form. The structure is compared with that of the oxidized S-S form as well as with that of the yeast SOD1 complexed with its copper chaperone, CCS. Local conformational rearrangements upon disulfide bridge reduction are localized in the region near Cys-57 that is completely exposed to the solvent in the present structure, at variance with the oxidized forms. There is a local disorder around Cys-57 that may serve for protein-protein recognition and may possibly be involved in intermolecular S-S bonds in familial amyotrophic lateral sclerosis-related SOD1 mutants. The structure allows us to further discuss the copper loading mechanism in SOD1.

PubMed: 16291742
DOI: 10.1074/jbc.M506497200

実験手法

SOLUTION NMR