1n0j

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(New page: 200px<br /> <applet load="1n0j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n0j, resolution 2.2&Aring;" /> '''The Structure of Hum...)
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<applet load="1n0j" size="450" color="white" frame="true" align="right" spinBox="true"
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'''The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals a Novel Tetrameric Interface of Two 4-Helix Bundles'''<br />
'''The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals a Novel Tetrameric Interface of Two 4-Helix Bundles'''<br />
==Overview==
==Overview==
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The 2.2 A resolution crystal structure of recombinant human manganese, superoxide dismutase, a homotetrameric enzyme that protects mitochondria, against oxygen-mediated free radical damage, has been determined. Within, each subunit, both the N-terminal helical hairpin and C-terminal, alpha/beta domains contribute ligands to the catalytic manganese site. Two, identical 4-helix bundles, symmetrically assembled from the N-terminal, helical hairpins, form novel tetrameric interfaces that stabilize the, active sites. Structurally altered polymorphic variants with reduced, activity, such as tetrameric interface mutant Ile-58 to Thr, may produce, not only an early selective advantage, through enhanced cytotoxicity of, tumor necrosis factor for virus-infected cells, but also detrimental, effects from increased mitochondrial oxidative damage, contributing to, degenerative conditions, including diabetes, aging, and Parkinson's and, Alzheimer's diseases.
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The 2.2 A resolution crystal structure of recombinant human manganese superoxide dismutase, a homotetrameric enzyme that protects mitochondria against oxygen-mediated free radical damage, has been determined. Within each subunit, both the N-terminal helical hairpin and C-terminal alpha/beta domains contribute ligands to the catalytic manganese site. Two identical 4-helix bundles, symmetrically assembled from the N-terminal helical hairpins, form novel tetrameric interfaces that stabilize the active sites. Structurally altered polymorphic variants with reduced activity, such as tetrameric interface mutant Ile-58 to Thr, may produce not only an early selective advantage, through enhanced cytotoxicity of tumor necrosis factor for virus-infected cells, but also detrimental effects from increased mitochondrial oxidative damage, contributing to degenerative conditions, including diabetes, aging, and Parkinson's and Alzheimer's diseases.
==About this Structure==
==About this Structure==
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1N0J 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 MN as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1ABM. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N0J OCA].
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1N0J 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=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1ABM. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N0J OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Superoxide dismutase]]
[[Category: Superoxide dismutase]]
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[[Category: Borgstahl, G.E.O.]]
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[[Category: Borgstahl, G E.O.]]
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[[Category: Parge, H.E.]]
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[[Category: Parge, H E.]]
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[[Category: Tainer, J.A.]]
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[[Category: Tainer, J A.]]
[[Category: MN]]
[[Category: MN]]
[[Category: four-helix bundle]]
[[Category: four-helix bundle]]
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[[Category: metalloenzyme]]
[[Category: metalloenzyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:16:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:56 2008''

Revision as of 12:00, 21 February 2008


1n0j, resolution 2.2Å

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The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals a Novel Tetrameric Interface of Two 4-Helix Bundles

Overview

The 2.2 A resolution crystal structure of recombinant human manganese superoxide dismutase, a homotetrameric enzyme that protects mitochondria against oxygen-mediated free radical damage, has been determined. Within each subunit, both the N-terminal helical hairpin and C-terminal alpha/beta domains contribute ligands to the catalytic manganese site. Two identical 4-helix bundles, symmetrically assembled from the N-terminal helical hairpins, form novel tetrameric interfaces that stabilize the active sites. Structurally altered polymorphic variants with reduced activity, such as tetrameric interface mutant Ile-58 to Thr, may produce not only an early selective advantage, through enhanced cytotoxicity of tumor necrosis factor for virus-infected cells, but also detrimental effects from increased mitochondrial oxidative damage, contributing to degenerative conditions, including diabetes, aging, and Parkinson's and Alzheimer's diseases.

About this Structure

1N0J is a Single protein structure of sequence from Homo sapiens with as ligand. This structure supersedes the now removed PDB entry 1ABM. Active as Superoxide dismutase, with EC number 1.15.1.1 Full crystallographic information is available from OCA.

Reference

The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles., Borgstahl GE, Parge HE, Hickey MJ, Beyer WF Jr, Hallewell RA, Tainer JA, Cell. 1992 Oct 2;71(1):107-18. PMID:1394426

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