Journal:JMB:2

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<b>Molecular Tour</b><br>
<b>Molecular Tour</b><br>
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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>.
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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<scene name='Journal:JMB:2/Scene_9/1'>TextToBeDisplayed</scene>. 2HQ makes contact with<scene name='Journal:JMB:2/Scene_10/3'>several catalytic residues</scene>(<scene name='Journal:JMB:2/Scene_10/2'>without labels</scene>)
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<scene name='Journal:JMB:2/Scene_7/1'>TextToBeDisplayed</scene>
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<scene name='Journal:JMB:2/Scene_8/1'>TextToBeDisplayed</scene>
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<scene name='Journal:JMB:2/Scene_9/1'>TextToBeDisplayed</scene>
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<scene name='Journal:JMB:2/Scene_10/3'>TextToBeDisplayed</scene>
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or without labels<scene name='Journal:JMB:2/Scene_10/2'>TextToBeDisplayed</scene>
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Figure   2.   Structural   details   of   the   2HQ/rePON1   complex   at   pH   6.5; <scene name='Journal:JMB:2/2a/5'> (A)</scene>   2HQ   and   the  
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structured  active-­site  loop  in  the  rePON1-­2HQ  complex  structure.  <scene name='Journal:JMB:2/2b/1'>(B)</scene>  Overlay  of  the  phosphate  ion  in  the  apo  rePON1  at  pH  6.5  and  of  2HQ  
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in  the  rePON1-­2HQ  complex.  <scene name='Journal:JMB:2/2c/1'>(C)</scene> The  first  segment  of  the  active-­site  loop,  and  residues  Y71  
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and  I74  in  particular,  comprises  part  of  PON1's  active-­site  wall.  <scene name='Journal:JMB:2/2d/3'>(D)</scene> Interactions  of  2HQ  with  
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active-­site  residues  (interactions  with  the  catalytic  Ca2+  are  highlighted  in  red).  
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<scene name='Journal:JMB:2/3/4'> Figure 3 </scene>.  Changes  in  the  rePON1  binding  site  upon  binding  of  2HQ.  Superimposition  of  the  
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rePON1-­2HQ  complex  (cyan; ''the  closed  conformation'')  with  the  apo  rePON1  structures  at  pH  
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4.5  (orange)  and  pH  6.5  (blue)  (''the  open  conformations'').  The  pH  4.5  conformation  prevents  
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closure  of  the  active-­site  loop  due  to  clashes  of  F347  and  H348  with  the  loop  residues  (e.g.  
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F77  and  I74).  Also  illustrated  is  the  movement  of  Y71  (dashed  arrow)  upon  binding  of  2HQ,  
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and  its  interaction  with  D183  in  the  2HQ  complex  structure.  
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<references/>
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Revision as of 21:38, 19 March 2012

rePON1 with 2HQ

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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()

  1. ↑ 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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