2c9v
From Proteopedia
(New page: 200px<br /> <applet load="2c9v" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c9v, resolution 1.07Å" /> '''ATOMIC RESOLUTION S...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2C9V is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CU, ZN, SO4 and NA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA]]. | + | 2C9V is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CU, ZN, SO4 and NA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: Superoxide dismutase]] | ||
[[Category: Antonyuk, S.]] | [[Category: Antonyuk, S.]] | ||
[[Category: Doucette, P.A.]] | [[Category: Doucette, P.A.]] | ||
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[[Category: zn superoxide dismutase]] | [[Category: zn superoxide dismutase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:03:41 2007'' |
Revision as of 10:58, 30 October 2007
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ATOMIC RESOLUTION STRUCTURE OF 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 ... [(full description)]
About this Structure
2C9V is a [Single protein] structure of sequence from [Homo sapiens] with CU, ZN, SO4 and NA as [ligands]. Active as [Superoxide dismutase], with EC number [1.15.1.1]. Structure known Active Site: AC1. 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 Tue Oct 30 13:03:41 2007
Categories: Homo sapiens | Single protein | Superoxide dismutase | Antonyuk, S. | Doucette, P.A. | Hasnain, S.S. | Hough, M.A. | Strange, R.W. | Valentine, J.S. | CU | NA | SO4 | ZN | Acetylation | Amyotrophic lateral sclerosis | Antioxidant | Copper | Disease mutation | Human cu | Metal-binding | Oxidoreductase | Oxioreductase | Zinc | Zn superoxide dismutase
