Group:SMART:2010 Pingry SMART Team: Difference between revisions
Florence Ma (talk | contribs) |
Florence Ma (talk | contribs) |
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Red and blue highlight the (alpha/beta)8 barrel structure typical of AKR's. | Red and blue highlight the (alpha/beta)8 barrel structure typical of AKR's. | ||
Cofactor ( | Cofactor (NADH) shown in wireframe and colored CPK. | ||
The backbone of the four residues changed between WT and NADP-binding mutant are colored orange (Lys232Gly, Phe22Tyr, Arg238His, Ala272Gly). | The backbone of the four residues changed between WT and NADP-binding mutant are colored orange (Lys232Gly, Phe22Tyr, Arg238His, Ala272Gly). | ||
Lys232Gly mutation is important because Gly has no sidechain so there is nothing to interact with the absent phosphate group. | |||
Phe22Tyr mutation reduces the Km for both NADPH and NADH. | |||
Arg238His mutation forms a pi-stacking interaction to stabilize the AKR with the cofactor. | |||
Ala272Gly mutation improves the kinetic properties by making it easier for the substrate to bind with the substrate or by improving the kinetics of cofactor binding and release. | |||
Other residues highlighted by displaying sidechain: | Other residues highlighted by displaying sidechain: | ||
Trp187; pi-stacking interaction with cofactor | Trp187; pi-stacking interaction with cofactor | ||
Not shown: | Not shown: | ||