title: Crystal structure of conjugated polyketone reductase (CPR-C1) from Candida parapsilosis IFO 0708 complexed with NADPH.
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.
authors.affiliation: Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
authors.forename: Hui-Min
authors.initials: HM
authors.lastname: Qin
authors.forename: Akihiro
authors.initials: A
authors.lastname: Yamamura
authors.forename: Takuya
authors.initials: T
authors.lastname: Miyakawa
authors.forename: Michihiko
authors.initials: M
authors.lastname: Kataoka
authors.forename: Shintaro
authors.initials: S
authors.lastname: Maruoka
authors.forename: Jun
authors.initials: J
authors.lastname: Ohtsuka
authors.forename: Koji
authors.initials: K
authors.lastname: Nagata
authors.forename: Sakayu
authors.initials: S
authors.lastname: Shimizu
authors.forename: Masaru
authors.initials: M
authors.lastname: Tanokura
mesh_terms: D002175:Candida / Q000201:enzymology*; D018360:Crystallography, X-Ray / Q000379:methods*; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism*; D009249:NADP
chemical_list: D005656:Fungal Proteins; D009249:NADP
keywords: NADPH; TIM barrel fold; aldo-keto reductases; d-pantoyl lactone; ketopantoyl lactone reductase