Succinate Dehydrogenase: Difference between revisions
Michael Vick (talk | contribs) No edit summary |
Michael Vick (talk | contribs) No edit summary |
||
| Line 14: | Line 14: | ||
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 and a binding site for succinate, while the latter is a 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> <ref name="abc">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 name="abc" /> <ref name="def">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 and a binding site for succinate, while the latter is a 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> <ref name="abc">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 name="abc" /> <ref name="def">PMID:16407191</ref>. | ||
===Binding sites=== | ===Binding sites=== | ||
| Line 25: | Line 24: | ||
<scene name='Michael_Vick_Sandbox_2/Sec_structure_ligs_colored/2'>ligands are color-coded</scene> as follows: orange indicates the FAD cofactor, green shows the Fe-S clusters, cyan indicates ubiquinone in its binding site, yellow shows Ca2+ ions, navy blue indicates oxaloacetate, pink is cardiolipin, brown is ephrin, and the heme group is indicated by the lime green structure. The exact function of some of these ligands with regard to succinate dehydrogenase remains unclear; ephrin, for example is suspected to be involved in certain cell signaling pathways in animal development <ref>PMID:11741094</ref>. | <scene name='Michael_Vick_Sandbox_2/Sec_structure_ligs_colored/2'>ligands are color-coded</scene> as follows: orange indicates the FAD cofactor, green shows the Fe-S clusters, cyan indicates ubiquinone in its binding site, yellow shows Ca2+ ions, navy blue indicates oxaloacetate, pink is cardiolipin, brown is ephrin, and the heme group is indicated by the lime green structure. The exact function of some of these ligands with regard to succinate dehydrogenase remains unclear; ephrin, for example is suspected to be involved in certain cell signaling pathways in animal development <ref>PMID:11741094</ref>. | ||
{{STRUCTURE_1nek | PDB=1nek | SCENE= }} | |||