3WG6

Crystal structure of conjugated polyketone reductase C1 from Candida parapsilosis complexed with NADPH

Summary for 3WG6

• Entry DOI: 10.2210/pdb3wg6/pdb
• Descriptor: Conjugated polyketone reductase C1, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• Functional Keywords: akr superfamily, tim barrel, oxidoreductase, d-pantoyl lactone
• Biological source: Candida parapsilosis (Yeast)
• Total number of polymer chains: 4
• Total formula weight: 142266.42

Authors

Qin, H.-M.,Yamamura, A.,Miyakawa, T.,Maruoka, S.,Ohtsuka, J.,Nagata, K.,Kataoka, M.,Shimizu, S.,Tanokura, M. (deposition date: 2013-07-28, release date: 2013-08-21, Last modification date: 2024-05-29)

Primary citation

Qin, H.M.,Yamamura, A.,Miyakawa, T.,Kataoka, M.,Maruoka, S.,Ohtsuka, J.,Nagata, K.,Shimizu, S.,Tanokura, M.
Crystal structure of conjugated polyketone reductase (CPR-C1) from Candida parapsilosis IFO 0708 complexed with NADPH.
Proteins, 81:2059-2063, 2013

PubMed Abstract: Conjugated polyketone reductase (CPR-C1) from Candida parapsilosis IFO 0708 is a member of the aldo-keto reductase (AKR) superfamily and reduces ketopantoyl lactone to d-pantoyl lactone in a NADPH-dependent and stereospecific manner. We determined the crystal structure of CPR-C1.NADPH complex at 2.20 Å resolution. CPR-C1 adopted a triose-phosphate isomerase (TIM) barrel fold at the core of the structure in which Thr25 and Lys26 of the GXGTX motif bind uniquely to the adenosine 2'-phosphate group of NADPH. This finding provides a novel structural basis for NADPH binding of the AKR superfamily.

PubMed: 23852710
DOI: 10.1002/prot.24363

Experimental method

X-RAY DIFFRACTION (2.2 Å)