KOPRI Repository

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

Cited 4 time in wos
Cited 5 time in scopus

Full metadata record

DC Field Value Language
dc.contributor.authorDo, Hackwon-
dc.contributor.authorKim, Il-Sup-
dc.contributor.authorKim, Young-Saeng-
dc.contributor.authorShin, Sun-Young-
dc.contributor.authorKim, Jin-Ju-
dc.contributor.authorMok, Ji-Eun-
dc.contributor.authorPark, Seong-Im-
dc.contributor.authorWi, Ah Ram-
dc.contributor.authorPark, Hyun-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorYoon, Ho-Sung-
dc.contributor.authorKim, Han-Woo-
dc.date.accessioned2017-08-03T13:33:36Z-
dc.date.available2017-08-03T13:33:36Z-
dc.date.issued2014-
dc.description.abstractMonodehydroascorbate 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 <em>Oryza sativa</em> L<em>. japonica </em>was expressed using <em>Escherichia coli </em>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<em> Acidovorax</em> sp. strain KKS102 (PDB entry 4h4q) as a model.-
dc.languageEnglish-
dc.subjectBiochemistry & Molecular Biology-
dc.subjectBiophysics-
dc.subjectCrystallography-
dc.titlePurification, characterization and preliminary X-ray crystallographic studies of monodehydroascorbate reductase from Oryza sativa L. japonica-
dc.typeArticle-
dc.identifier.bibliographicCitationDo, Hackwon, et al. 2014. "Purification, characterization and preliminary X-ray crystallographic studies of monodehydroascorbate reductase from Oryza sativa L. japonica". <em>Acta Crystallographica,</em>, F(70): 1244-1248.-
dc.citation.titleActa Crystallographica,-
dc.citation.volumeF-
dc.citation.number70-
dc.citation.page1244-1248.-
dc.identifier.doi10.1107/S2053230X14015908-
dc.subject.keywordMonodehydroascorbate reductase-
dc.subject.keywordOryza sativa L. japonica-
dc.subject.keywordReactive oxygen species-
dc.identifier.scopusid2-s2.0-84907032400-
dc.identifier.wosid000341818600024-
Appears in Collections  
2014-2016, Antarctic Organisms: Cold-Adaptation Mechanism and Its Application (14-16) / Park; Hyun (PE14070; PE15070; PE16070)
Files in This Item

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse