1q0g: Difference between revisions
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[[Image:1q0g.gif|left|200px]] | [[Image:1q0g.gif|left|200px]] | ||
'''Crystal structure of Ni-containing superoxide dismutase with Ni-ligation corresponding to the state after full x-ray-induced reduction''' | {{Structure | ||
|PDB= 1q0g |SIZE=350|CAPTION= <scene name='initialview01'>1q0g</scene>, resolution 1.60Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</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] | |||
|GENE= | |||
}} | |||
'''Crystal structure of Ni-containing superoxide dismutase with Ni-ligation corresponding to the state after full x-ray-induced reduction''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1Q0G is a [ | 1Q0G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_seoulensis Streptomyces seoulensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q0G OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of nickel-containing superoxide dismutase reveals another type of active site., Wuerges J, Lee JW, Yim YI, Yim HS, Kang SO, Djinovic Carugo K, Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8569-74. Epub 2004 Jun 1. PMID:[http:// | Crystal structure of nickel-containing superoxide dismutase reveals another type of active site., Wuerges J, Lee JW, Yim YI, Yim HS, Kang SO, Djinovic Carugo K, Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8569-74. Epub 2004 Jun 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15173586 15173586] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces seoulensis]] | [[Category: Streptomyces seoulensis]] | ||
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[[Category: NI]] | [[Category: NI]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: homohexamer of four-helix | [[Category: homohexamer of four-helix bundle]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:31:23 2008'' | ||
Revision as of 14:31, 20 March 2008
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| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Ni-containing superoxide dismutase with Ni-ligation corresponding to the state after full x-ray-induced reduction
OverviewOverview
Superoxide dismutases (SODs, EC 1.15.1.1) are ubiquitous enzymes that efficiently catalyze the dismutation of superoxide radical anions to protect biological molecules from oxidative damage. The crystal structure of nickel-containing SOD (NiSOD) from Streptomyces seoulensis was determined for the resting, x-ray-reduced, and thiosulfate-reduced enzyme state. NiSOD is a homohexamer consisting of four-helix-bundle subunits. The catalytic center resides in the N-terminal active-site loop, where a Ni(III) ion is coordinated by the amino group of His-1, the amide group of Cys-2, two thiolate groups of Cys-2 and Cys-6, and the imidazolate of His-1 as axial ligand that is lost in the chemically reduced state as well as after x-ray-induced reduction. This structure represents a third class of SODs concerning the catalytic metal species, subunit structure, and oligomeric organization. It adds a member to the small number of Ni-metalloenzymes and contributes with its Ni(III) active site to the general understanding of Ni-related biochemistry. NiSOD is shown to occur also in bacteria other than Streptomyces and is predicted to be present in some cyanobacteria.
About this StructureAbout this Structure
1Q0G is a Single protein structure of sequence from Streptomyces seoulensis. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of nickel-containing superoxide dismutase reveals another type of active site., Wuerges J, Lee JW, Yim YI, Yim HS, Kang SO, Djinovic Carugo K, Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8569-74. Epub 2004 Jun 1. PMID:15173586
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