1sox

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Revision as of 03:24, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1sox" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sox, resolution 1.9Å" /> '''SULFITE OXIDASE FROM ...)
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File:1sox.gif


1sox, resolution 1.9Å

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SULFITE OXIDASE FROM CHICKEN LIVER

OverviewOverview

The molybdenum-containing enzyme sulfite oxidase catalyzes the conversion, of sulfite to sulfate, the terminal step in the oxidative degradation of, cysteine and methionine. Deficiency of this enzyme in humans usually leads, to major neurological abnormalities and early death. The crystal structure, of chicken liver sulfite oxidase at 1.9 A resolution reveals that each, monomer of the dimeric enzyme consists of three domains. At the active, site, the Mo is penta-coordinated by three sulfur ligands, one oxo group, and one water/hydroxo. A sulfate molecule adjacent to the Mo identifies, the substrate binding pocket. Four variants associated with sulfite, oxidase deficiency have been identified: two mutations are near the, sulfate binding site, while the other mutations occur within the domain, mediating dimerization.

About this StructureAbout this Structure

1SOX is a Single protein structure of sequence from Gallus gallus with SO4, MTE, MO, HEM, EPE and GOL as ligands. Active as Sulfite oxidase, with EC number 1.8.3.1 Full crystallographic information is available from OCA.

ReferenceReference

Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase., Kisker C, Schindelin H, Pacheco A, Wehbi WA, Garrett RM, Rajagopalan KV, Enemark JH, Rees DC, Cell. 1997 Dec 26;91(7):973-83. PMID:9428520

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