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Crystal structure of conjugated polyketone reductase (CPR‐C1) from Candida parapsilosis IFO 0708 complexed with NADPH
Author(s) -
Qin HuiMin,
Yamamura Akihiro,
Miyakawa Takuya,
Kataoka Michihiko,
Maruoka Shintaro,
Ohtsuka Jun,
Nagata Koji,
Shimizu Sakayu,
Tanokura Masaru
Publication year - 2013
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24363
Subject(s) - candida parapsilosis , conjugated system , chemistry , microbiology and biotechnology , antifungal , organic chemistry , biology , polymer
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. Proteins 2013; 81:2059–2063. © 2013 Wiley Periodicals, Inc.