Journal:JMB:2
From Proteopedia
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| - | < | + | <StructureSection load="Workbench_test2.pdb" size="500" color="white" frame="true" align="right" caption="rePON1 with 2HQ" scene="Journal:JMB:2/Opening/4" /> |
=== Catalytic versatility and backups in enzyme active sites: The case of serum paraoxanase 1 === | === Catalytic versatility and backups in enzyme active sites: The case of serum paraoxanase 1 === | ||
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Previously PON1 was <scene name='Journal:JMB:2/Scene_1/3'>solved at 4.5 pH</scene>. The authors sought a physiologically active pH and <scene name='Journal:JMB:2/Scene_2/1'>solved PON1 at 6.5 pH (overlain with 4.5)</scene>. Note <scene name='Journal:JMB:2/Scene_3/1'>residues 346-348 in the two structures</scene>. Especially, observe the <scene name='Journal:JMB:2/Scene_4/1'>movement of residue 71</scene>. The authors also solved PON1 at 6.5 pH in <scene name='Journal:JMB:2/Scence_5/3'>complex with 2HQ (a lactone approximate)</scene>. Here, the authors 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>. In summary, there are <scene name='Journal:JMB:2/Scene_10/3'>several differences between PON1 with complex(cyan), without at 6.5(blue) and at 4.5(orange)</scene> (<scene name='Journal:JMB:2/Scene_10/2'>without labels</scene>) | Previously PON1 was <scene name='Journal:JMB:2/Scene_1/3'>solved at 4.5 pH</scene>. The authors sought a physiologically active pH and <scene name='Journal:JMB:2/Scene_2/1'>solved PON1 at 6.5 pH (overlain with 4.5)</scene>. Note <scene name='Journal:JMB:2/Scene_3/1'>residues 346-348 in the two structures</scene>. Especially, observe the <scene name='Journal:JMB:2/Scene_4/1'>movement of residue 71</scene>. The authors also solved PON1 at 6.5 pH in <scene name='Journal:JMB:2/Scence_5/3'>complex with 2HQ (a lactone approximate)</scene>. Here, the authors 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>. In summary, there are <scene name='Journal:JMB:2/Scene_10/3'>several differences between PON1 with complex(cyan), without at 6.5(blue) and at 4.5(orange)</scene> (<scene name='Journal:JMB:2/Scene_10/2'>without labels</scene>) | ||
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| + | </StructureSection> | ||
<references/> | <references/> | ||
__NOEDITSECTION__ | __NOEDITSECTION__ | ||
Revision as of 15:16, 20 March 2012
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Catalytic versatility and backups in enzyme active sites: The case of serum paraoxanase 1
Moshe Ben-David, Mikael Elias, Jean-Jacques Filippi, Elisabet Dunach, Israel Silman, Joel Sussman and Dan Tawfik, PhD [1]
Molecular Tour
Previously PON1 was . The authors sought a physiologically active pH and . Note . Especially, observe the . The authors also solved PON1 at 6.5 pH in . Here, the authors for the first time observe ordered . The residues colored red . , suggesting that lactone adopt a similar position. 2HQ makes contact with . In summary, there are ()
</StructureSection>
- ↑ 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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