2AF2
Solution structure of disulfide reduced and copper depleted Human Superoxide Dismutase
Summary for 2AF2
| Entry DOI | 10.2210/pdb2af2/pdb |
| NMR Information | BMRB: 6821 |
| Descriptor | Superoxide dismutase [Cu-Zn], ZINC ION (2 entities in total) |
| Functional Keywords | human superoxide dismutase, solution structure, homodimeric protein, disulfide bond reduced, copper depleted protein, structural genomics, structural proteomics in europe, spine, oxidoreductase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P00441 |
| Total number of polymer chains | 2 |
| Total formula weight | 31689.68 |
| Authors | Banci, L.,Bertini, I.,Cantini, F.,D'Amelio, N.,Gaggelli, E.,Structural Proteomics in Europe (SPINE) (deposition date: 2005-07-25, release date: 2005-11-15, Last modification date: 2024-05-29) |
| Primary citation | 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 Cited by 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: 16291742DOI: 10.1074/jbc.M506497200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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