2c9u
From Proteopedia
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|PDB= 2c9u |SIZE=350|CAPTION= <scene name='initialview01'>2c9u</scene>, resolution 1.24Å | |PDB= 2c9u |SIZE=350|CAPTION= <scene name='initialview01'>2c9u</scene>, resolution 1.24Å | ||
|SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+F'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+F'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9u OCA], [http://www.ebi.ac.uk/pdbsum/2c9u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c9u RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
Human Cu-Zn superoxide dismutase (SOD1) protects cells from the effects of oxidative stress. Mutations in SOD1 are linked to the familial form of amyotrophic lateral sclerosis. Several hypotheses for their toxicity involve the mis-metallation of the enzyme. We present atomic-resolution crystal structures and biophysical data for human SOD1 in three metallation states: Zn-Zn, Cu-Zn and as-isolated. These data represent the first atomic-resolution structures for human SOD1, the first structure of a reduced SOD1, and the first structure of a fully Zn-substituted SOD1 enzyme. Recombinantly expressed as-isolated SOD1 contains a mixture of Zn and Cu at the Cu-binding site. The Zn-Zn structure appears to be at least as stable as the correctly (Cu-Zn) metallated enzyme. These data raise the possibility that in a cellular environment with low availability of free copper, Zn-Zn may be the preferred metallation state of SOD1 prior to its interaction with the copper chaperone. | Human Cu-Zn superoxide dismutase (SOD1) protects cells from the effects of oxidative stress. Mutations in SOD1 are linked to the familial form of amyotrophic lateral sclerosis. Several hypotheses for their toxicity involve the mis-metallation of the enzyme. We present atomic-resolution crystal structures and biophysical data for human SOD1 in three metallation states: Zn-Zn, Cu-Zn and as-isolated. These data represent the first atomic-resolution structures for human SOD1, the first structure of a reduced SOD1, and the first structure of a fully Zn-substituted SOD1 enzyme. Recombinantly expressed as-isolated SOD1 contains a mixture of Zn and Cu at the Cu-binding site. The Zn-Zn structure appears to be at least as stable as the correctly (Cu-Zn) metallated enzyme. These data raise the possibility that in a cellular environment with low availability of free copper, Zn-Zn may be the preferred metallation state of SOD1 prior to its interaction with the copper chaperone. | ||
| - | |||
| - | ==Disease== | ||
| - | Known disease associated with this structure: Amyotrophic lateral sclerosis, due to SOD1 deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147450 147450]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Strange, R W.]] | [[Category: Strange, R W.]] | ||
[[Category: Valentine, J S.]] | [[Category: Valentine, J S.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: ZN]] | ||
[[Category: acetylation]] | [[Category: acetylation]] | ||
[[Category: amyotrophic lateral sclerosis]] | [[Category: amyotrophic lateral sclerosis]] | ||
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[[Category: zn superoxide dismutase]] | [[Category: zn superoxide dismutase]] | ||
| - | ''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 02:18:29 2008'' |
Revision as of 23:18, 30 March 2008
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| , resolution 1.24Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS-ISOLATED CU-ZN HUMAN SUPEROXIDE DISMUTASE
Overview
Human Cu-Zn superoxide dismutase (SOD1) protects cells from the effects of oxidative stress. Mutations in SOD1 are linked to the familial form of amyotrophic lateral sclerosis. Several hypotheses for their toxicity involve the mis-metallation of the enzyme. We present atomic-resolution crystal structures and biophysical data for human SOD1 in three metallation states: Zn-Zn, Cu-Zn and as-isolated. These data represent the first atomic-resolution structures for human SOD1, the first structure of a reduced SOD1, and the first structure of a fully Zn-substituted SOD1 enzyme. Recombinantly expressed as-isolated SOD1 contains a mixture of Zn and Cu at the Cu-binding site. The Zn-Zn structure appears to be at least as stable as the correctly (Cu-Zn) metallated enzyme. These data raise the possibility that in a cellular environment with low availability of free copper, Zn-Zn may be the preferred metallation state of SOD1 prior to its interaction with the copper chaperone.
About this Structure
2C9U is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes., Strange RW, Antonyuk SV, Hough MA, Doucette PA, Valentine JS, Hasnain SS, J Mol Biol. 2006 Mar 10;356(5):1152-62. Epub 2005 Dec 12. PMID:16406071
Page seeded by OCA on Mon Mar 31 02:18:29 2008
Categories: Homo sapiens | Single protein | Superoxide dismutase | Antonyuk, S. | Doucette, P A. | Hasnain, S S. | Hough, M A. | Strange, R W. | Valentine, J S. | Acetylation | Amyotrophic lateral sclerosis | Antioxidant | Copper | Disease mutation | Human cu | Metal-binding | Oxidoreductase | Zinc | Zn superoxide dismutase
