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Crystallization and preliminary X-ray crystallographic studies of dehydroascorbate reductase (DHAR) from Oryza sativa L. japonica

Cited 1 time in wos
Cited 1 time in scopus

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dc.contributor.authorIl-Sup Kim-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorYoon, Ho-Sung-
dc.contributor.authorKim, Han-Woo-
dc.contributor.authorPark, Hyun-
dc.contributor.authorWi, Ah Ram-
dc.contributor.authorSeong-Im Park-
dc.contributor.authorJi-Eun Mok-
dc.contributor.authorJin-Ju Kim-
dc.contributor.authorSun-Young Shin-
dc.contributor.authorDo, Hackwon-
dc.contributor.authorYoung-Saeng Kim-
dc.date.accessioned2018-03-29T06:01:03Z-
dc.date.available2018-03-29T06:01:03Z-
dc.date.issued2014-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/7268-
dc.description.abstractDehydroascorbate reductase from Oryza sativa L. japonica (OsDHAR), a key enzyme in the regeneration of vitamin C, maintains reduced pools of ascorbic acid to detoxify reactive oxygen species (ROS). In previous studies, the overexpression of OsDHAR in transgenic rice increased grain yield and biomass as well as the amount of ascorbate, suggesting that ascorbate levels are directly associated with crop production in rice. Hence, the increased level of antioxidants generated by OsDHAR has been speculated to protect rice from oxidative damage and increase the yield of germination. However, the crystal structure and detailed mechanisms of this important enzyme need to be further elucidated. In this study, recombinant OsDHAR protein was purified and crystallized using the sitting-drop vapor diffusion method at pH 8.0 and 298 K. Plate-shape crystals were obtained using 0.15 M potassium bromide and 30% (w/v) PEG MME 2000 as a precipitant, and the crystals diffracted to a resolution of 1.9 A at beamline 5C of the Pohang Accelerator Laboratory. The X-ray diffraction data indicated that the crystal contained one OsDHAR molecule in the asymmetric unit with the space group P21 (unit-cell parameters, a = 47.03, b = 48.38, c = 51.83 A, and β = 107.41°).-
dc.languageEnglish-
dc.titleCrystallization and preliminary X-ray crystallographic studies of dehydroascorbate reductase (DHAR) from Oryza sativa L. japonica-
dc.title.alternative벼유래 dehydroascorbate reductase (DHAR) 효소의 결정화 및 삼차구조해석을 위한 X-선 회절데이타 분석-
dc.typeArticle-
dc.identifier.bibliographicCitationIl-Sup Kim, et al. 2014. "Crystallization and preliminary X-ray crystallographic studies of dehydroascorbate reductase (DHAR) from Oryza sativa L. japonica". <em>ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS</em>, 70(6): 781-785.-
dc.citation.titleACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS-
dc.citation.volume70-
dc.citation.number6-
dc.identifier.doi10.1107/S2053230X14009133-
dc.citation.startPage781-
dc.citation.endPage785-
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2012:95.862-
dc.subject.keywordOryza sativa L. japonica-
dc.subject.keywordX-ray crystallography-
dc.subject.keywordascorbate-
dc.subject.keyworddehydroascorbate reductase-
dc.identifier.localId2014-0062-
dc.identifier.scopusid2-s2.0-84905455778-
dc.identifier.wosid000337062500020-
Appears in Collections  
2014-2016, Antarctic Organisms: Cold-Adaptation Mechanism and Its Application (14-16) / Park; Hyun (PE14070; PE15070; PE16070)
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