1MJ4

Crystal Structure Analysis of the cytochrome b5 domain of human sulfite oxidase

Summary for 1MJ4

• Entry DOI: 10.2210/pdb1mj4/pdb
• Related: 1SOX
• Descriptor: sulfite oxidase, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• Functional Keywords: cytochrome b5, heme, sulfite oxidase, oxidoreductase
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion intermembrane space: P51687
• Total number of polymer chains: 1
• Total formula weight: 9891.77

Authors

Rudolph, M.J.,Johnson, J.L.,Rajagopalan, K.V.,Kisker, C. (deposition date: 2002-08-26, release date: 2002-09-12, Last modification date: 2024-02-14)

Primary citation

Rudolph, M.J.,Johnson, J.L.,Rajagopalan, K.V.,Kisker, C.
The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain.
Acta Crystallogr.,Sect.D, 59:1183-1191, 2003

PubMed Abstract: 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.

PubMed: 12832761
DOI: 10.1107/S0907444903009934

Experimental method

X-RAY DIFFRACTION (1.2 Å)