Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 70, Issue -, Pages 1244-1248Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X14015908
Keywords
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Funding
- Antarctic Organisms Cold-Adaptation Mechanisms and its application grant - Korea Polar Research Institute, Kyungpook National University Research Fund [PE14070]
- Next Generation BioGreen 21 Program (Rural Development Administration, Republic of Korea) [PJ008115012014]
- Korea Institute of Marine Science & Technology Promotion (KIMST) [PE14070] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- Rural Development Administration (RDA), Republic of Korea [PJ008115012014] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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 angstrom resolution and contained one molecule in the asymmetric unit (the Matthews coefficient V-M is 1.98 angstrom(3) Da(-1), corresponding to a solvent content of 38.06%) in space group P4(1)2(1)2 with unit-cell parameters a = b = 81.89, c = 120.4 angstrom. 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.
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