Phosphoglycerate Kinase: Difference between revisions
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The bilobed nature of the protein is very crucial in the its catlytic function. The active site is broken into two pieces, one on each interior lobe. On one site the ADP-Mg2+ substrate binds and on the other lobe the 1,3-Biphosphoglycerate substrate binds. Upon binding of both substrates at the active sites, the protein's conformation changes such that the two lobes of the protein swing together. The hinge for this conformational change is beta sheet L and the new conformation is formed via a salt bridge between ARG62 and ASP200. This swinging shut of the protein creates an interior hydrophobic chamber that is free of water for the reaction to take place in. | The bilobed nature of the protein is very crucial in the its catlytic function. The active site is broken into two pieces, one on each interior lobe. On one site the ADP-Mg2+ substrate binds and on the other lobe the 1,3-Biphosphoglycerate substrate binds. Upon binding of both substrates at the active sites, the protein's conformation changes such that the two lobes of the protein swing together. The hinge for this conformational change is beta sheet L and the new conformation is formed via a salt bridge between ARG62 and ASP200. This swinging shut of the protein creates an interior hydrophobic chamber that is free of water for the reaction to take place in. | ||
<scene name='Shane_Harmon_Sandbox/Atp/1'>Ligand</scene> | |||
Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load | Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load | ||
and display another structure. | and display another structure. | ||
