Structural highlights
Publication Abstract from PubMed
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 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Qin HM, 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. 2013 Jul 15. doi: 10.1002/prot.24363. PMID:23852710 doi:10.1002/prot.24363
