Journal:JMB:2
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Previously PON1 was <scene name='Journal:JMB:2/Scene_2/2'>solved at 4.5 pH</scene>. We sought a physiologically active pH and <scene name='Journal:JMB:2/Scene_2/3'>solved PON1 at 6.5 pH (overlain with 4.5)</scene>. Note <scene name='Journal:JMB:2/Scene_3/2'>residues 346-348 in the two structures</scene>. Especially, observe the <scene name='Journal:JMB:2/Scene_4/1'>movement of residue 71</scene>. We also solved PON1 at 6.5 pH in <scene name='Journal:JMB:2/Scence_5/3'>complex with 2HQ (a lactone approximate)</scene>. Here, we for the first time observe ordered <scene name='Journal:JMB:2/Scene_6/1'>active site loop density</scene>. The residues colored red <scene name='Journal:JMB:2/Scene_7/1'>contact the active site</scene>. <scene name='Journal:JMB:2/Scene_8/1'>2HQ overlaps with PO4</scene>, suggesting that lactone adopt a similar position. 2HQ makes contact with <scene name='Journal:JMB:2/Scene_9/1'>several catalytic residues</scene>. | Previously PON1 was <scene name='Journal:JMB:2/Scene_2/2'>solved at 4.5 pH</scene>. We sought a physiologically active pH and <scene name='Journal:JMB:2/Scene_2/3'>solved PON1 at 6.5 pH (overlain with 4.5)</scene>. Note <scene name='Journal:JMB:2/Scene_3/2'>residues 346-348 in the two structures</scene>. Especially, observe the <scene name='Journal:JMB:2/Scene_4/1'>movement of residue 71</scene>. We also solved PON1 at 6.5 pH in <scene name='Journal:JMB:2/Scence_5/3'>complex with 2HQ (a lactone approximate)</scene>. Here, we for the first time observe ordered <scene name='Journal:JMB:2/Scene_6/1'>active site loop density</scene>. The residues colored red <scene name='Journal:JMB:2/Scene_7/1'>contact the active site</scene>. <scene name='Journal:JMB:2/Scene_8/1'>2HQ overlaps with PO4</scene>, suggesting that lactone adopt a similar position. 2HQ makes contact with <scene name='Journal:JMB:2/Scene_9/1'>several catalytic residues</scene>. | ||
Revision as of 20:31, 21 March 2012
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- ↑ Ben-David M, Elias M, Filippi JJ, Dunach E, Silman I, Sussman JL, Tawfik DS. Catalytic Versatility and Backups in Enzyme Active Sites: The Case of Serum Paraoxonase 1. J Mol Biol. 2012 Mar 1. PMID:22387469 doi:10.1016/j.jmb.2012.02.042
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