| http://purl.uniprot.org/citations/27067046 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27067046 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27067046 | http://www.w3.org/2000/01/rdf-schema#comment | "Dehydroascorbate reductase (DHAR), a member of the glutathione-S-transferase (GST) family, reduces dehydroascorbate (DHA) to ascorbate (AsA; Vitamin-C) in a glutathione (GSH)-dependent manner and in doing so, replenishes the critical AsA pool of the cell. To understand the enzyme mechanism in detail, we determined the crystal structure of a plant DHAR from Pennisetum glaucum (PgDHAR) using Iodide-Single Anomalous Dispersion (SAD) and Molecular replacement methods, in two different space groups. Here, we show PgDHAR in complex with two non-native ligands, viz. an acetate bound at the G-site, which resembles the γ-carboxyl moiety of GSH, and a glycerol at the H-site, which shares the backbone of AsA. We also show that, in the absence of bound native substrates, these non-native ligands help define the critical 'hook points' in the DHAR enzyme active site. Further, our data suggest that these non-native ligands can act as the logical bootstrapping points for iterative design of inhibitors/analogs for DHARs."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2016.04.031"xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2016.04.031"xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/author | "Kumar A."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/author | "Kumar A."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/author | "Reddy M.K."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/author | "Reddy M.K."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/author | "Arockiasamy A."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/author | "Arockiasamy A."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/author | "Jain S.K."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/author | "Jain S.K."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/author | "Mahanty S."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/author | "Mahanty S."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/author | "Krishna Das B."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/author | "Krishna Das B."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/author | "Maindola P."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/author | "Maindola P."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/name | "Biochem Biophys Res Commun"xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/pages | "1152-1157"xsd:string |
| http://purl.uniprot.org/citations/27067046 | http://purl.uniprot.org/core/pages | "1152-1157"xsd:string |