2af2: Difference between revisions
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[[Image:2af2.gif|left|200px]]< | [[Image:2af2.gif|left|200px]] | ||
'''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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| 2af2 | |||||||||||||
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| Ligands: | ZN | ||||||||||||
| 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
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
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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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
