2af2
From Proteopedia
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|PDB= 2af2 |SIZE=350|CAPTION= <scene name='initialview01'>2af2</scene> | |PDB= 2af2 |SIZE=350|CAPTION= <scene name='initialview01'>2af2</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2af2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2af2 OCA], [http://www.ebi.ac.uk/pdbsum/2af2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2af2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Gaggelli, E.]] | [[Category: Gaggelli, E.]] | ||
[[Category: SPINE, Structural Proteomics in Europe.]] | [[Category: SPINE, Structural Proteomics in Europe.]] | ||
| - | [[Category: ZN]] | ||
[[Category: copper depleted protein]] | [[Category: copper depleted protein]] | ||
[[Category: disulfide bond reduced]] | [[Category: disulfide bond reduced]] | ||
| Line 43: | Line 45: | ||
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:51:47 2008'' |
Revision as of 22:51, 30 March 2008
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| Ligands: | |||||||
| Gene: | SOD1 (Homo sapiens) | ||||||
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Mon Mar 31 01:51:47 2008
Categories: Homo sapiens | Single protein | Superoxide dismutase | Amelio, N D. | Banci, L. | Bertini, I. | Cantini, F. | Gaggelli, E. | SPINE, Structural Proteomics in Europe. | Copper depleted protein | Disulfide bond reduced | Homodimeric protein | Human superoxide dismutase | Nmr | Solution structure | Spine | Structural genomic | Structural proteomics in europe
