2af2
From Proteopedia
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| - | [[Image:2af2.gif|left|200px]]< | + | [[Image:2af2.gif|left|200px]] |
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| - | '''Solution structure of disulfide reduced and copper depleted Human Superoxide Dismutase''' | + | {{Structure |
| + | |PDB= 2af2 |SIZE=350|CAPTION= <scene name='initialview01'>2af2</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] | ||
| + | |GENE= SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Solution structure of disulfide reduced and copper depleted Human Superoxide Dismutase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2AF2 is a [ | + | 2AF2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AF2 OCA]. |
==Reference== | ==Reference== | ||
| - | Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form., Banci L, Bertini I, Cantini F, D'Amelio N, Gaggelli E, J Biol Chem. 2006 Jan 27;281(4):2333-7. Epub 2005 Nov 14. PMID:[http:// | + | Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form., Banci L, Bertini I, Cantini F, D'Amelio N, Gaggelli E, J Biol Chem. 2006 Jan 27;281(4):2333-7. Epub 2005 Nov 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16291742 16291742] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: solution structure]] | [[Category: solution structure]] | ||
[[Category: spine]] | [[Category: spine]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:48:52 2008'' |
Revision as of 13:48, 20 March 2008
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| Ligands: | |||||||
| Gene: | SOD1 (Homo sapiens) | ||||||
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of disulfide reduced and copper depleted Human Superoxide Dismutase
Contents |
Overview
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.
Disease
Known disease associated with this structure: Amyotrophic lateral sclerosis, due to SOD1 deficiency OMIM:[147450]
About this Structure
2AF2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form., Banci L, Bertini I, Cantini F, D'Amelio N, Gaggelli E, J Biol Chem. 2006 Jan 27;281(4):2333-7. Epub 2005 Nov 14. PMID:16291742
Page seeded by OCA on Thu Mar 20 15:48:52 2008
Categories: Homo sapiens | Single protein | Superoxide dismutase | Amelio, N D. | Banci, L. | Bertini, I. | Cantini, F. | Gaggelli, E. | SPINE, Structural Proteomics in Europe. | ZN | Copper depleted protein | Disulfide bond reduced | Homodimeric protein | Human superoxide dismutase | Nmr | Solution structure | Spine | Structural genomic | Structural proteomics in europe
