Group:SMART:2010 Pingry SMART Team: Difference between revisions
From Proteopedia
Jump to navigationJump to search
| Line 109: | Line 109: | ||
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 <scene name='2010_Pingry_SMART_Team/1mi3_default/4'>Glu227</scene> changes so both of the oxygens on its sidechain | The <scene name='2010_Pingry_SMART_Team/1mi3_default/4'>Glu227</scene> changes so both of the oxygens on its sidechain form interactions with the 2' and 3' alcohol groups on the ribose of NAD+, while only one of the oxygens on the Glu227 interacted with the 3' alcohol group on the ribose of NADP+. | ||
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. | 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. | ||
