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. | 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'>some 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. | |||
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. | ||
