Sandbox Reserved 1802: Difference between revisions
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== Other Important Features == | == Other Important Features == | ||
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. <scene name='95/954099/Cleft/ | Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree.<scene name='95/954099/Cleft/7'> Deep cleft in center of enzyme.</scene> <scene name='95/954099/Cleft/4'>A different view of the deep cleft.</scene> <scene name='95/954099/Cleft/5'>Opening and Closing of the VFT fold.</scene> | ||
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. | Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. | ||
