1mj4

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(New page: 200px<br /> <applet load="1mj4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mj4, resolution 1.20&Aring;" /> '''Crystal Structure A...)
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Revision as of 16:05, 12 November 2007


1mj4, resolution 1.20Å

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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 SO4, HEM and GOL 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

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