3vxg

Crystal structure of conjugated polyketone reductase C2 from Candida Parapsilosis

spinqualitylabelsall models 3vxg, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vxg is a 1 chain structure with sequence from Atcc 22019. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4h8n Gene: cpr-c2 (ATCC 22019) Activity: 2-dehydropantolactone reductase ((Si)-specific), with EC number 1.1.1.214 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Conjugated polyketone reductase C2 (CPR-C2) from Candida parapsilosis IFO 0708, identified as a nicotinamide adenine dinucleotide phosphate (NADPH)-dependent ketopantoyl lactone reductase, belongs to the aldo-keto reductase superfamily. This enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner. To elucidate the structural basis of the substrate specificity, we determined the crystal structures of the apo CPR-C2 and CPR-C2/NADPH complex at 1.70 and 1.80 A resolutions, respectively. CPR-C2 adopted a triose-phosphate isomerase barrel fold at the core of the structure. Binding with the cofactor NADPH induced conformational changes in which Thr27 and Lys28 moved 15 and 5.0 A, respectively, in the close vicinity of the adenosine 2'-phosphate group of NADPH to form hydrogen bonds. Based on the comparison of the CPR-C2/NADPH structure with 3-alpha-hydroxysteroid dehydrogenase and mutation analyses, we constructed substrate binding models with ketopantoyl lactone, which provided insight into the substrate specificity by the cofactor-induced structure. The results will be useful for the rational design of CPR-C2 mutants targeted for use in the industrial manufacture of ketopantoyl lactone. Structure of conjugated polyketone reductase from Candida parapsilosis IFO 0708 reveals conformational changes for substrate recognition upon NADPH binding.,Qin HM, Yamamura A, Miyakawa T, Kataoka M, Nagai T, Kitamura N, Urano N, Maruoka S, Ohtsuka J, Nagata K, Shimizu S, Tanokura M Appl Microbiol Biotechnol. 2013 Jul 5. PMID:23828603 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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