   1.1.1.358 | more |
docking analysis and structure homology modeling of CorCPR, the crystal structure of CPR-C2 from Candida parapsilosis strain IFO 0708 (PDB ID 3VXG, resolution 1.7 A) is used as the model structure, overview. KPL is docked into the substrate binding pocket. The model predicts that the C3 carbonyl oxygen of KPL forms hydrogen bond with the side chains of Tyr63, and the alpha-amino group of Thr27 also forms a hydrogen bond with C2 carbonyl oxygen. The catalytic tetrads of CorCPR are Asp58, Tyr63, Lys88 and His125. Tyr63 acts as a general acid, and His125 facilitates proton donation, the phenolic hydroxy group of Tyr63 provide general acid catalytic assistance to carbonyl group of KPL, and residues Asp 58 and Tys88 are responsible for the hydrogen transfer. The stereospecificity of CorCPR is respected to the pro-R hydrogen at C4 of the nicotinamide ring and the pseudo re-side attack of the hydride on the carbonyl group. In addition, the formation of hydrogen bond between Thr27 and the C2 carbonyl oxygen of KPL plays an important role in substrate recognition |
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