3wg6
From Proteopedia
Crystal structure of conjugated polyketone reductase C1 from Candida parapsilosis complexed with NADPH
Structural highlights
FunctionCPRC1_CANPA NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. Reduces ketopantoyl lactone (2-dehydropantolactone) and isatin. Does not act on menadione, p-nitrobenzaldehyde and pyridine-3-aldehyde.[1] [2] Publication Abstract from PubMedConjugated 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 A 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. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc. Crystal structure of conjugated polyketone reductase (CPR-C1) from Candida parapsilosis IFO 0708 complexed with NADPH.,Qin HM, Yamamura A, Miyakawa T, Kataoka M, Maruoka S, Ohtsuka J, Nagata K, Shimizu S, Tanokura M Proteins. 2013 Jul 15. doi: 10.1002/prot.24363. PMID:23852710[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Candida parapsilosis | Large Structures | Kataoka M | Maruoka S | Miyakawa T | Nagata K | Ohtsuka J | Qin H-M | Shimizu S | Tanokura M | Yamamura A
