4H8N
Crystal structure of conjugated polyketone reductase C2 from candida parapsilosis complexed with NADPH
Summary for 4H8N
| Entry DOI | 10.2210/pdb4h8n/pdb |
| Related | 3VXG |
| Descriptor | Conjugated polyketone reductase C2, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | oxidoreductase, tim barrel, d-pantoyl lactone |
| Biological source | Candida parapsilosis (Yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 71443.99 |
| Authors | Qin, H.-M.,Yamamura, A.,Miyakawa, T.,Maruoka, S.,Ohtsuka, J.,Nagata, K.,Kataoka, M.,Shimizu, S.,Tanokura, M. (deposition date: 2012-09-23, release date: 2013-08-07, Last modification date: 2023-11-08) |
| Primary citation | Qin, H.-M.,Yamamura, A.,Miyakawa, T.,Kataoka, M.,Nagai, T.,Kitamura, N.,Urano, N.,Maruoka, S.,Ohtsuka, J.,Nagata, K.,Shimizu, S.,Tanokura, M. Structure of conjugated polyketone reductase from Candida parapsilosis IFO 0708 reveals conformational changes for substrate recognition upon NADPH binding Appl.Microbiol.Biotechnol., 98:243-249, 2014 Cited by PubMed Abstract: Conjugated polyketone reductase C2 (CPR-C2) from Candida parapsilosis IFO 0708, identified as a nicotinamide adenine dinucleotide phosphate (NADPH)-dependent ketopantoyl lactone reductase, belongs to the aldo-keto reductase superfamily. This enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner. To elucidate the structural basis of the substrate specificity, we determined the crystal structures of the apo CPR-C2 and CPR-C2/NADPH complex at 1.70 and 1.80 Å resolutions, respectively. CPR-C2 adopted a triose-phosphate isomerase barrel fold at the core of the structure. Binding with the cofactor NADPH induced conformational changes in which Thr27 and Lys28 moved 15 and 5.0 Å, respectively, in the close vicinity of the adenosine 2'-phosphate group of NADPH to form hydrogen bonds. Based on the comparison of the CPR-C2/NADPH structure with 3-α-hydroxysteroid dehydrogenase and mutation analyses, we constructed substrate binding models with ketopantoyl lactone, which provided insight into the substrate specificity by the cofactor-induced structure. The results will be useful for the rational design of CPR-C2 mutants targeted for use in the industrial manufacture of ketopantoyl lactone. PubMed: 23828603DOI: 10.1007/s00253-013-5073-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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