Journal:JMB:2

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<b>Molecular Tour</b><br>
<b>Molecular Tour</b><br>
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Figure   2.   Structural   details   of   the   2HQ/rePON1   complex   at   pH   6.5;;   (A)<scene name='Journal:JMB:2/2a/4'>TextToBeDisplayed</scene>   2HQ   and   the  
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Figure   2.   Structural   details   of   the   2HQ/rePON1   complex   at   pH   6.5; <scene name='Journal:JMB:2/2a/4'> (A)</scene>   2HQ   and   the  
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structured  active-­site  loop  in  the  rePON1-­2HQ  complex  structure.  The  Fo-­Fc  omit  map  is  
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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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contouered  at   B)<scene name='Journal:JMB:2/2b/1'>TextToBeDisplayed</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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in  the  rePON1-­2HQ  complex.  (C)  <scene name='Journal:JMB:2/2c/1'>TextToBeDisplayed</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/2'>(D)</scene> Interactions  of  2HQ  with  
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and  I74  in  particular,  comprises  part  of  PON1's  active-­site  wall.  (D)  <scene name='Journal:JMB:2/2d/2'>TextToBeDisplayed</scene>Interactions  of  2HQ  with  
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active-­site  residues  (interactions  with  the  catalytic  Ca2+  are  highlighted  in  red).  
active-­site  residues  (interactions  with  the  catalytic  Ca2+  are  highlighted  in  red).  
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Figure  3.  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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Revision as of 17:11, 6 March 2012

caption

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Title Of The Paper

Authors[1]


Molecular Tour
Figure   2.   Structural   details   of   the   2HQ/rePON1   complex   at   pH   6.5;   2HQ   and   the   structured  active-­site  loop  in  the  rePON1-­2HQ  complex  structure.    Overlay  of  the  phosphate  ion  in  the  apo  rePON1  at  pH  6.5  and  of  2HQ   in  the  rePON1-­2HQ  complex.   The  first  segment  of  the  active-­site  loop,  and  residues  Y71   and  I74  in  particular,  comprises  part  of  PON1's  active-­site  wall.   Interactions  of  2HQ  with   active-­site  residues  (interactions  with  the  catalytic  Ca2+  are  highlighted  in  red).  

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