Sandbox Reserved 1717: Difference between revisions
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==Catalytic Cysteines== | ===Catalytic Cysteines=== | ||
A set of four cysteines is consistently conserved in all VKOR homologs. In the human homolog (HsVKOR) these cysteines are Cys43, Cys51, Cys132, and Cys 135. <scene name='90/904321/Cysteines/6'>Significant Cysteines</scene> In the Pufferfish homolog (TrVKORL) these cysteines, due to Cryo-EM differences,are Cys52, Cys55, Cys141, and Cys144. These cysteines are the key factor that allow for Vitamin K Epoxide Reductase to perform its function, which is to open the epoxide ring on Vitamin K Epoxide in order to re-make Vitamin K Quinone. In the closed conformation, that is induced when Vitamin K binds in the hydrophobic pocket, Cys-132 binds to Cys-51 and Cys-135 will bind to the 3' hydroxyl group on Vitamin K Epoxide, which allows for the electron transfer to open up the epoxide ring. <scene name='90/904321/Cys52disulfidecys55/9'>Electron Transfer through Cysteine138 TrVKORL</scene> | A set of four cysteines is consistently conserved in all VKOR homologs. In the human homolog (HsVKOR) these cysteines are Cys43, Cys51, Cys132, and Cys 135. <scene name='90/904321/Cysteines/6'>Significant Cysteines</scene> In the Pufferfish homolog (TrVKORL) these cysteines, due to Cryo-EM differences,are Cys52, Cys55, Cys141, and Cys144. These cysteines are the key factor that allow for Vitamin K Epoxide Reductase to perform its function, which is to open the epoxide ring on Vitamin K Epoxide in order to re-make Vitamin K Quinone. In the closed conformation, that is induced when Vitamin K binds in the hydrophobic pocket, Cys-132 binds to Cys-51 and Cys-135 will bind to the 3' hydroxyl group on Vitamin K Epoxide, which allows for the electron transfer to open up the epoxide ring. <scene name='90/904321/Cys52disulfidecys55/9'>Electron Transfer through Cysteine138 TrVKORL</scene> | ||
