Flexibility of aromatic residues in acetylcholinesterase: Difference between revisions

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Yechun Xu, Eran Hodis, Joel L. Sussman, David Canner, Michal Harel

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 == Flexibility of aromatic residues in the active-gorge of AChE ==
-The high aromatic content of the deep and narrow active-site gorge of acetylcholinesterase (AChE) is a remarkable feature of this enzyme.There are <scene name='Flexibility_of_aromatic_residues_in_acetylcholinesterase/14_residues/6'>14 conserved aromatic amino acids</scene> lined along the gorge of ''Torpedo californica'' AChE (TcAChE), F120, F288, F290, F330, F331, W84, W233, W279, W432, Y70, Y121, Y130, Y334, and Y442. The side-chain conformational analyses based on the multuple available crystal structures and molecular dyanmics (MD) simulation trajectories show that the degree of flexibility of these 14 aromatic side chains is diverse. While those of <scene name='Flexibility_of_aromatic_residues_in_acetylcholinesterase/W279_f330/2'>F330 and W279 </scene>are both very flexible, the side-chain conformations of <scene name='Flexibility_of_aromatic_residues_in_acetylcholinesterase/Groupii/3'>F120, W233, W432, Y70, Y121, F288, F290 and F331</scene> appear to be fixed. Residues located on, or adjacent to the <scene name='Flexibility_of_aromatic_residues_in_acetylcholinesterase/Omega_loop/1'>omega-loop (C67-C94)</scene>, viz. <scene name='Flexibility_of_aromatic_residues_in_acetylcholinesterase/Groupiii/3'>W84, Y130, Y442, and Y334</scene>, display different flexibilities in the MD simulations and in the crystal structures.
+The high aromatic content of the deep and narrow active-site gorge of acetylcholinesterase (AChE) is a remarkable feature of this enzyme.There are <scene name='Flexibility_of_aromatic_residues_in_acetylcholinesterase/14_residues/6'>14 conserved aromatic amino acids</scene> lined along the gorge of ''Torpedo californica'' AChE (TcAChE), F120, F288, F290, F330, F331, W84, W233, W279, W432, Y70, Y121, Y130, Y334, and Y442. The side-chain conformational analyses based on the multuple available crystal structures and molecular dyanmics (MD) simulation trajectories show that the degree of flexibility of these 14 aromatic side chains is diverse. While those of <scene name='Flexibility_of_aromatic_residues_in_acetylcholinesterase/W279_f330/2'>F330 and W279 </scene>are both very flexible, the side-chain conformations of <scene name='Flexibility_of_aromatic_residues_in_acetylcholinesterase/Groupii/3'>F120, W233, W432, Y70, Y121, F288, F290 and F331</scene> appear to be fixed. Residues located on, or adjacent to the <scene name='Flexibility_of_aromatic_residues_in_acetylcholinesterase/Omega_loop/1'>omega-loop (C67-C94)</scene>, viz. <scene name='Flexibility_of_aromatic_residues_in_acetylcholinesterase/Groupiii/4'>W84, Y130, Y442, and Y334</scene>, display different flexibilities in the MD simulations and in the crystal structures.
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