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Purification, characterization and preliminary X-ray crystallographic studies of monodehydroascorbate reductase from Oryza sativa L. japonica

Cited 5 time in scopus
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Title
Purification, characterization and preliminary X-ray crystallographic studies of monodehydroascorbate reductase from Oryza sativa L. japonica
Other Titles
Oryza saltiva L. japonica 유래 MDHAR의 정제, 특성 및 preliminary X-ray crystallographic 연구
Authors
박승임
목지은
김진주
신선영
Kim, Young-Saeng
Kim, Il-Sup
Do, Hackwon
Kim, Han-Woo
Yoon, Ho-Sung
Lee, Jun Hyuck
Park, Hyun
Wi, Ah Ram
Keywords
Monodehydroascorbate reductase; Oryza sativa L. japonica; reactive oxygen species
Issue Date
2014
Citation
박승임, et al. 2014. "Purification, characterization and preliminary X-ray crystallographic studies of monodehydroascorbate reductase from Oryza sativa L. japonica". Acta Crystallographica Section F: Structural Biology Communications, 70(9): 1244-1248.
Abstract
Monodehydroascorbate reductase (MDHAR;EC 1.6.5.4) is a key enzyme in the reactive oxygen species (ROS) detoxification system of plants. The participation of MDHAR in ascorbate (AsA) recycling in the ascorbate?glutathione cycle is important in the acquired tolerance of crop plants to abiotic environmental stresses. Thus, MDHAR represents a strategic target protein for the improvement of crop yields. Although physiological studies have intensively characterized MDHAR, a structure-based functional analysis is not available. Here, a cytosolic MDHAR (OsMDHAR) derived from Oryza sativa L. japonica was expressed using Escherichia coli strain NiCo21 (DE3) and purified. The purified OsMDHAR showed specific enzyme activity (approximately 380 U per milligram of protein) and was crystallized using the hanging-drop vapourdiffusion method at pH 8.0 and 298 K. The crystal diffracted to 1.9 A ˚ resolution and contained one molecule in the asymmetric unit (the Matthews coefficient VM is 1.98 A ˚ 3 Da 1, corresponding to a solvent content of 38.06%) in space group P41212 with unit-cell parameters a = b = 81.89, c = 120.4 A ˚ . The phase of the OsMDHAR structure was resolved by the molecular-replacement method using a ferredoxin reductase from Acidovorax sp. strain KKS102 (PDB entry 4h4q) as a model.
URI
http://repository.kopri.re.kr/handle/201206/7282
DOI
http://dx.doi.org/10.1107/S2053230X14015908
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