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© Marie Prévost, Institut Pasteur
Image of a portion of a Xenopus oocyte expressing a channel receptor.
Publication : Biochemical and biophysical research communications

Non-native ligands define the active site of Pennisetum glaucum (L.) R. Br dehydroascorbate reductase

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Biochemical and biophysical research communications - 09 Apr 2016

Krishna Das B, Kumar A, Maindola P, Mahanty S, Jain SK, Reddy MK, Arockiasamy A

Link to Pubmed [PMID] – 27067046

Biochem. Biophys. Res. Commun. 2016 05;473(4):1152-1157

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.

https://www.ncbi.nlm.nih.gov/pubmed/27067046