5d9v

Crystal structure of oxidized dehydroascorbate reductase (OsDHAR) from Oryza sativa L. japonica

spinqualitylabelsall models 5d9v, resolution 1.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5d9v is a 1 chain structure with sequence from Oryza sativa Japonica Group. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.69Å Ligands: CA, OCS, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DHAR1_ORYSJ Involved in ascorbate homeostasis. Maintains redox pools of ascorbate by recycling dihydroascorbate (DHA) to ascorbate (Probable). Involved in scavenging reactive oxygen species (ROS) under oxidative stresses. Possesses dehydroascorbate reductase (DHAR) activity in vitro (PubMed:19011360). May function via a ping-pong reaction mechanism with an electron transfer at the active site (PubMed:26775680). Possesses chaperone-like activity in vitro (PubMed:26775680). Publication Abstract from PubMed Dehydroascorbate reductase (DHAR) is a key enzyme involved in the recycling of ascorbate, which catalyses the glutathione (GSH)-dependent reduction of oxidized ascorbate (dehydroascorbate, DHA). As a result, DHAR regenerates a pool of reduced ascorbate and detoxifies reactive oxygen species (ROS). In previous experiments involving transgenic rice, we observed that overexpression of DHAR enhanced grain yield and biomass. Since the structure of DHAR is not available, the enzymatic mechanism is not well-understood and remains poorly characterized. To elucidate the molecular basis of DHAR catalysis, we determined the crystal structures of DHAR from Oryza sativa L. japonica (OsDHAR) in the native, ascorbate-bound, and GSH-bound forms and refined their resolutions to 1.9, 1.7, and 1.7 A, respectively. These complex structures provide the first information regarding the location of the ascorbate and GSH binding sites and their interacting residues. The location of the ascorbate-binding site overlaps with the GSH-binding site, suggesting a ping-pong kinetic mechanism for electron transfer at the common Cys20 active site. Our structural information and mutagenesis data provide useful insights into the reaction mechanism of OsDHAR against ROS-induced oxidative stress in rice. Structural understanding of the recycling of oxidized ascorbate by dehydroascorbate reductase (OsDHAR) from Oryza sativa L. japonica.,Do H, Kim IS, Jeon BW, Lee CW, Park AK, Wi AR, Shin SC, Park H, Kim YS, Yoon HS, Kim HW, Lee JH Sci Rep. 2016 Jan 18;6:19498. doi: 10.1038/srep19498. PMID:26775680 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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