Sandbox Reserved 164: Difference between revisions

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{{Sandbox_Reserved_Irma_Santoro_7}}
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<Structure load='3ECU' size='500' frame='true' align='right' caption='Crystal Structure of SOD 1 protein, PDB ID: 3ECU' scene='Insert optional scene name here' />
<Structure load='3ECU' size='500' frame='true' align='right' caption='Crystal Structure of SOD 1 protein, PDB ID: 3ECU' scene='Insert optional scene name here' />
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== Superoxide Dismutase 1 (SOD 1) ==
== Superoxide Dismutase 1 (SOD 1) ==
SOD1 is one of three oxidoreductase enzymes that is responsible for binding copper and zinc ions to highly reactive oxygen free radicals and transforming them into oxygen and hydrogen peroxide <ref name="McCord">McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049-55. PMID:5389100</ref>. This occurs in a quick two step mechanism  
SOD1 is one of three oxidoreductase enzymes that is responsible for binding copper and zinc ions to highly reactive oxygen free radicals and transforming them into oxygen and hydrogen peroxide. <ref name="McCord">McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049-55. PMID:5389100</ref>  This occurs in a quick two step mechanism:


M(n+1)+-SOD + O2− → Mn+-SOD + O2
M(n+1)+-SOD + O2− → Mn+-SOD + O2
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Mn+-SOD + O2− + 2H+ → M(n+1)+-SOD + H2O2<ref name="Tainer">Tainer JA, Getzoff ED, Richardson JS, Richardson DC. Structure and mechanism of copper, zinc superoxide dismutase. Nature. 1983 Nov 17-23;306(5940):284-7. PMID:6316150</ref>.
Mn+-SOD + O2− + 2H+ → M(n+1)+-SOD + H2O2<ref name="Tainer">Tainer JA, Getzoff ED, Richardson JS, Richardson DC. Structure and mechanism of copper, zinc superoxide dismutase. Nature. 1983 Nov 17-23;306(5940):284-7. PMID:6316150</ref>.


This protein is coded for by the SOD 1 gene located on chromosome 21 at position 21q22.1 from base pairs 33,031,934 to 33,041,243 <ref name="Sod1">SOD 1.  Genetics Home Reference.  U.S. National Library of Medicine; 2010</ref>.
This protein is coded for by the SOD 1 gene located on chromosome 21 at position 21q22.1 from base pairs 33,031,934 to 33,041,243. <ref name="Sod1">SOD 1.  Genetics Home Reference.  U.S. National Library of Medicine; 2010</ref>




== Structure ==
== Structure ==
The SOD 1 protein is a homodimer with an amino acid sequence length of 154.  SOD 1 has an 8-stranded "Greek key" beta-barrel shape with the active site located between the barrels.  The copper and zinc ligands are made up of six histidine side-chains and one aspartate side-chain with the metal ions connected with by a single histidine chain.<ref name="Tainer">Tainer JA, Getzoff ED, Richardson JS, Richardson DC. Structure and mechanism of copper, zinc superoxide dismutase. Nature. 1983 Nov 17-23;306(5940):284-7. PMID:6316150</ref>. This first SOD structure was determined by Irwin Fridovich and Joe McCord in 1973 <ref name="McCord">McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049-55. PMID:5389100</ref><ref name="McCord2">McCord JM, Fridovich I. Superoxide dismutase: the first twenty years (1968-1988). Free Radic Biol Med. 1988;5(5-6):363-9. PMID:2855736</ref> with the SOD 1 "Greek key" structure visualized by Dr. Jane Richardson (see below).<ref name="Tainer">Tainer JA, Getzoff ED, Richardson JS, Richardson DC. Structure and mechanism of copper, zinc superoxide dismutase. Nature. 1983 Nov 17-23;306(5940):284-7. PMID:6316150</ref>
The SOD 1 protein is a homodimer with an amino acid sequence length of 154.  SOD 1 has an 8-stranded "Greek key" beta-barrel shape with the active site located between the barrels.  The copper and zinc ligands are made up of six histidine side-chains and one aspartate side-chain with the metal ions connected with by a single histidine chain.<ref name="Tainer">Tainer JA, Getzoff ED, Richardson JS, Richardson DC. Structure and mechanism of copper, zinc superoxide dismutase. Nature. 1983 Nov 17-23;306(5940):284-7. PMID:6316150</ref> This first SOD structure was determined by Irwin Fridovich and Joe McCord in 1973 <ref name="McCord">McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049-55. PMID:5389100</ref><ref name="McCord2">McCord JM, Fridovich I. Superoxide dismutase: the first twenty years (1968-1988). Free Radic Biol Med. 1988;5(5-6):363-9. PMID:2855736</ref> with the SOD 1 "Greek key" structure visualized by Dr. Jane Richardson (see below).<ref name="Tainer">Tainer JA, Getzoff ED, Richardson JS, Richardson DC. Structure and mechanism of copper, zinc superoxide dismutase. Nature. 1983 Nov 17-23;306(5940):284-7. PMID:6316150</ref>
[[Image:601px-2SOD ribbon pastel.jpg|300px|left]]
[[Image:601px-2SOD ribbon pastel.jpg|300px|left]]


== ALS ==
== ALS ==
Mutations to the SOD 1 protein have been linked to the development of familial amyotrophic lateral sclerosis. <ref name="Al-Chalabi">Al-Chalabi A, Leigh PN (August 2000). "Recent advances in amyotrophic lateral sclerosis". Curr. Opin. Neurol. 13 (4): 397–405. PMID 10970056.</ref> 




== References ==
== References ==
<references />
<references />
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