Succinate Dehydrogenase: Difference between revisions
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===Structure=== | ===Structure=== | ||
The tetramer is composed of two hydrophilic and two hydrophobic subunits. The hydrophilic subunits are named SdhA (PDB = [[2wdq]]) and SdhB; the former is a flavoprotein containing a covalently-bound FAD cofactor a binding site for succinate, while the latter is Fe-S protein bearing the three iron-sulfur clusters 2Fe-2S, 3Fe-4S, and 4Fe-4S. The hydrophobic subunits, termed SdhC and SdhD, anchor the protein in the mitochondrial membrane and formally comprise cytochrome b <ref>PMID:12966066</ref> and <ref>PMID:12560550</ref>. This cytochrome contains six transmembrane α-helices, a heme b group, and a binding site for ubiquinone located in a space bounded by SdhB, SdhC, and SdhD <ref>PMID:12560550</ref> and <ref>PMID:16407191</ref>. | The tetramer is composed of <scene name='Michael_Vick_Sandbox_2/2wdv_hydrophob_and_polar/1'>two hydrophilic and two hydrophobic subunits</scene>. The hydrophilic subunits are named SdhA (PDB = [[2wdq]]) and SdhB; the former is a flavoprotein containing a covalently-bound FAD cofactor a binding site for succinate, while the latter is Fe-S protein bearing the three iron-sulfur clusters 2Fe-2S, 3Fe-4S, and 4Fe-4S. The hydrophobic subunits, termed SdhC and SdhD, anchor the protein in the mitochondrial membrane and formally comprise cytochrome b <ref>PMID:12966066</ref> and <ref>PMID:12560550</ref>. This cytochrome contains six transmembrane α-helices, a heme b group, and a binding site for ubiquinone located in a space bounded by SdhB, SdhC, and SdhD <ref>PMID:12560550</ref> and <ref>PMID:16407191</ref>. | ||
{{STRUCTURE_1nek | PDB=1nek | SCENE=2wdv_sec_structure }} | {{STRUCTURE_1nek | PDB=1nek | SCENE=2wdv_sec_structure }} | ||