1SOX

SULFITE OXIDASE FROM CHICKEN LIVER

Summary for 1SOX

• Entry DOI: 10.2210/pdb1sox/pdb
• Descriptor: SULFITE OXIDASE, SULFATE ION, PHOSPHONIC ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)ESTER, ... (8 entities in total)
• Functional Keywords: oxidoreductase, sulfite oxidation
• Biological source: Gallus gallus (chicken)
• Cellular location: Mitochondrion intermembrane space: P07850
• Total number of polymer chains: 2
• Total formula weight: 104932.58

Authors

Kisker, C.,Schindelin, H.,Rees, D.C. (deposition date: 1997-12-31, release date: 1998-04-29, Last modification date: 2024-05-22)

Primary citation

Kisker, C.,Schindelin, H.,Pacheco, A.,Wehbi, W.A.,Garrett, R.M.,Rajagopalan, K.V.,Enemark, J.H.,Rees, D.C.
Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase.
Cell(Cambridge,Mass.), 91:973-983, 1997

PubMed Abstract: 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.

PubMed: 9428520
DOI: 10.1016/S0092-8674(00)80488-2

Experimental method

X-RAY DIFFRACTION (1.9 Å)