Group:SMART:2010 Pingry SMART Team: Difference between revisions

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As with the previous protein, pink and blue highlight the alpha and beta barrel structure common to AKR's. The cofactor NAD+ is shown in wireframe and colored CPK.

In xylose reductases' binding to NAD+, because of conformational changes on loops, <scene name='2010_Pingry_SMART_Team/1mi3_default/3'>two sidechains no longer interact with the cofactor</scene>. Lys274 and Ser275(highlighted in blue) no longer interact significantly with the NAD+. Instead, only Glu227, Asn276, and Arg280 (highlighted in green) bind to the cofactor.

In xylose reductases' binding to NAD+, because of conformational changes on loops, <scene name='2010_Pingry_SMART_Team/1mi3_default/3'>two sidechains no longer interact with the cofactor</scene>. Lys274 and Ser275(highlighted in blue) no longer interact significantly with the NAD+. Instead, only Glu227, Asn276, and Arg280 (highlighted in green) bind to the cofactor. The Glu227 changes so only one of the oxygens on its sidechain forms a water-mediated interaction with the NAD+, while on NADP+ both oxygens interacted.

While xylose reductase prefers to utilize NADP+, it is able to accommodate the absence of the 2'-phosphate by adapting different conformations. <scene name='2010_Pingry_SMART_Team/1mi3_default/2'>Asn276</scene> shifts to Hydrogen bond with the hydroxy group of the NAD+ in place of the phosphate group.

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 As with the previous protein, pink and blue highlight the alpha and beta barrel structure common to AKR's.  The cofactor NAD+ is shown in wireframe and colored CPK.
-In xylose reductases' binding to NAD+, because of conformational changes on loops, <scene name='2010_Pingry_SMART_Team/1mi3_default/3'>two sidechains no longer interact with the cofactor</scene>.  Lys274 and Ser275(highlighted in blue) no longer interact significantly with the NAD+.  Instead, only Glu227, Asn276, and Arg280 (highlighted in green) bind to the cofactor.
+In xylose reductases' binding to NAD+, because of conformational changes on loops, <scene name='2010_Pingry_SMART_Team/1mi3_default/3'>two sidechains no longer interact with the cofactor</scene>.  Lys274 and Ser275(highlighted in blue) no longer interact significantly with the NAD+.  Instead, only Glu227, Asn276, and Arg280 (highlighted in green) bind to the cofactor. The Glu227 changes so only one of the oxygens on its sidechain forms a water-mediated interaction with the NAD+, while on NADP+ both oxygens interacted.
 While xylose reductase prefers to utilize NADP+, it is able to accommodate the absence of the 2'-phosphate by adapting different conformations.  <scene name='2010_Pingry_SMART_Team/1mi3_default/2'>Asn276</scene> shifts to Hydrogen bond with the hydroxy group of the NAD+ in place of the phosphate group.
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