1mj4
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The molybdenum- and iron-containing enzyme sulfite oxidase catalyzes the | + | The molybdenum- and iron-containing enzyme sulfite oxidase catalyzes the physiologically vital oxidation of sulfite to sulfate. Sulfite oxidase contains three domains: an N-terminal cytochrome b(5) domain, a central domain harboring the molybdenum cofactor (Moco) and a C-terminal dimerization domain. Oxidation of the substrate sulfite is coupled to the transfer of two electrons to the molybdenum cofactor. Subsequently, these electrons are passed on, one at a time, to the b(5) heme of sulfite oxidase and from there to the soluble electron carrier cytochrome c. The crystal structure of the oxidized human sulfite oxidase cytochrome b(5) domain has been determined at 1.2 A resolution and has been refined to a crystallographic R factor of 0.107 (R(free) = 0.137). A comparison of this structure with other b(5)-type cytochromes reveals distinct structural features present in the sulfite oxidase b(5) domain which promote optimal electron transport between the Moco of sulfite oxidase and the heme of cytochrome c. |
==Disease== | ==Disease== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sulfite oxidase]] | [[Category: Sulfite oxidase]] | ||
| - | [[Category: Johnson, J | + | [[Category: Johnson, J L.]] |
[[Category: Kisker, C.]] | [[Category: Kisker, C.]] | ||
| - | [[Category: Rajagopalan, K | + | [[Category: Rajagopalan, K V.]] |
| - | [[Category: Rudolph, M | + | [[Category: Rudolph, M J.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: sulfite oxidase]] | [[Category: sulfite oxidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:39 2008'' |
Revision as of 11:55, 21 February 2008
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Crystal Structure Analysis of the cytochrome b5 domain of human sulfite oxidase
Contents |
Overview
The molybdenum- and iron-containing enzyme sulfite oxidase catalyzes the physiologically vital oxidation of sulfite to sulfate. Sulfite oxidase contains three domains: an N-terminal cytochrome b(5) domain, a central domain harboring the molybdenum cofactor (Moco) and a C-terminal dimerization domain. Oxidation of the substrate sulfite is coupled to the transfer of two electrons to the molybdenum cofactor. Subsequently, these electrons are passed on, one at a time, to the b(5) heme of sulfite oxidase and from there to the soluble electron carrier cytochrome c. The crystal structure of the oxidized human sulfite oxidase cytochrome b(5) domain has been determined at 1.2 A resolution and has been refined to a crystallographic R factor of 0.107 (R(free) = 0.137). A comparison of this structure with other b(5)-type cytochromes reveals distinct structural features present in the sulfite oxidase b(5) domain which promote optimal electron transport between the Moco of sulfite oxidase and the heme of cytochrome c.
Disease
Known disease associated with this structure: Sulfite oxidase deficiency OMIM:[606887]
About this Structure
1MJ4 is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Sulfite oxidase, with EC number 1.8.3.1 Full crystallographic information is available from OCA.
Reference
The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain., Rudolph MJ, Johnson JL, Rajagopalan KV, Kisker C, Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1183-91. Epub 2003, Jun 27. PMID:12832761
Page seeded by OCA on Thu Feb 21 13:55:39 2008
Categories: Homo sapiens | Single protein | Sulfite oxidase | Johnson, J L. | Kisker, C. | Rajagopalan, K V. | Rudolph, M J. | GOL | HEM | SO4 | Cytochrome b5 | Heme
