2c9v

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[[Image:2c9v.gif|left|200px]]<br /><applet load="2c9v" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2c9v.gif|left|200px]]
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caption="2c9v, resolution 1.07&Aring;" />
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'''ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE'''<br />
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{{Structure
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|PDB= 2c9v |SIZE=350|CAPTION= <scene name='initialview01'>2c9v</scene>, resolution 1.07&Aring;
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|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+F'>AC1</scene>
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
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|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]
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|GENE=
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}}
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'''ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=NA:'>NA</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+F'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA].
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2C9V 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=2C9V OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16406071 16406071]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16406071 16406071]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: zn superoxide dismutase]]
[[Category: zn superoxide dismutase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:46:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:12:53 2008''

Revision as of 14:12, 20 March 2008

Image:2c9v.gif


PDB ID 2c9v

Drag the structure with the mouse to rotate
, resolution 1.07Å
Sites:
Ligands: , , and
Activity: Superoxide dismutase, with EC number 1.15.1.1
Coordinates: save as pdb, mmCIF, xml



ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE


Contents

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.

Disease

Known disease associated with this structure: Amyotrophic lateral sclerosis, due to SOD1 deficiency OMIM:[147450]

About this Structure

2C9V 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

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