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2af2

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[[Image:2af2.gif|left|200px]]
[[Image:2af2.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2af2 |SIZE=350|CAPTION= <scene name='initialview01'>2af2</scene>
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The line below this paragraph, containing "STRUCTURE_2af2", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE= SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_2af2| PDB=2af2 | SCENE= }}
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|RELATEDENTRY=
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|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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'''Solution structure of disulfide reduced and copper depleted Human Superoxide Dismutase'''
'''Solution structure of disulfide reduced and copper depleted Human Superoxide Dismutase'''
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[[Category: Gaggelli, E.]]
[[Category: Gaggelli, E.]]
[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: SPINE, Structural Proteomics in Europe.]]
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[[Category: copper depleted protein]]
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[[Category: Copper depleted protein]]
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[[Category: disulfide bond reduced]]
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[[Category: Disulfide bond reduced]]
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[[Category: homodimeric protein]]
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[[Category: Homodimeric protein]]
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[[Category: human superoxide dismutase]]
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[[Category: Human superoxide dismutase]]
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[[Category: nmr]]
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[[Category: Nmr]]
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[[Category: solution structure]]
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[[Category: Solution structure]]
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[[Category: spine]]
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[[Category: Spine]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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[[Category: structural proteomics in europe]]
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[[Category: Structural proteomics in europe]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:17:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:51:47 2008''
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Revision as of 05:17, 13 April 2008

Image:2af2.gif

Template:STRUCTURE 2af2

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 Sun Apr 13 08:17:10 2008

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