Succinate Dehydrogenase: Difference between revisions
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<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 | SIZE=400| SCENE= |right|CAPTION=Succinate dehydrogenase complex with FAD, protoporphyrin, ubiquinone, oxaloacetate, Ca+2 ion, cardiolipin, Fe2S2, Fe3S4, Fe4S4, [[1nek]] }} | |||
===Mechanisms=== | ===Mechanisms=== | ||