Group:SMART:2010 Pingry SMART Team: Difference between revisions
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'''Design description''' | '''Design description''' | ||
The conformation of 2,5-DKGR (diketo-d-gluconic acid reductase)is a parallel alpha/beta barrel of <scene name='2010_Pingry_SMART_Team/1m9h_original/14'>eight alpha helices (highlighted red) and eight beta sheets (highlighted blue).</scene> Notably, the alpha/beta 8 barrel structure is demonstrated by other enzymes of the aldo-keto reductase family. | |||
<scene name='2010_Pingry_SMART_Team/1m9h_original/16'>Mutations of 2.5-DKGR's conformation have been conducted to alternate the cofactor specificity to NADH rather than NADPH. Alternate cofactor (NADH)for mutant 2,5 DKGR shown in wireframe and colored CPK.</scene> | |||
The backbone of the four residues changed between WT and NADP-binding mutant are colored orange <scene name='2010_Pingry_SMART_Team/1m9h_original/17'>(Lys232Gly, Phe22Tyr, Arg238His, Ala272Gly).</scene> | The backbone of the four residues changed between WT and NADP-binding mutant are colored orange <scene name='2010_Pingry_SMART_Team/1m9h_original/17'>(Lys232Gly, Phe22Tyr, Arg238His, Ala272Gly).</scene> |