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dc.contributor.author신동해-
dc.date.accessioned2016-08-28T10:08:05Z-
dc.date.available2016-08-28T10:08:05Z-
dc.date.issued2012-
dc.identifier.issn1744-3091-
dc.identifier.otherOAK-9504-
dc.identifier.urihttp://dspace.ewha.ac.kr/handle/2015.oak/223220-
dc.description.abstractATktA is the most critical enzyme in the nonoxidative pentose phosphate pathway. It catalyzes the conversion of xylulose 5-phosphate and ribose 5 - phosphate into sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate, and its products are used in the biosynthesis of acetyl-CoA, aromatic amino acids, nucleic acids and ADP-l-glycero-β-d-manno-heptose. TktA also has an unexpected role in chromosome structure that is independent of its metabolic responsibilities. Therefore, it is a new potent antibiotic target. In this study, TktA from Burkholderia pseudomallei has been cloned, expressed, purified and crystallized. Synchrotron X-ray data were also collected to 2.0 A resolution. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a = 146.2, b = 74.6, c = 61.6 A, β = 113.0°. A full structural determination is under way in order to provide insight into the structure-function relationship of this protein. © 2012. © 2012 International Union of Crystallography All rights reserved.-
dc.languageEnglish-
dc.titleA preliminary X-ray study of transketolase from Burkholderia pseudomallei-
dc.typeArticle-
dc.relation.issue12-
dc.relation.volume68-
dc.relation.indexSCOPUS-
dc.relation.startpage1554-
dc.relation.lastpage1556-
dc.relation.journaltitleActa Crystallographica Section F: Structural Biology and Crystallization Communications-
dc.identifier.doi10.1107/S1744309112044375-
dc.identifier.wosidWOS:000311693300029-
dc.identifier.scopusid2-s2.0-84870925001-
dc.author.googleKim M.-S.-
dc.author.googleLim A.-
dc.author.googleYang S.W.-
dc.author.googleLee D.-
dc.author.googlePark J.-
dc.author.googleShin D.H.-
dc.contributor.scopusid신동해(15920079700)-
dc.date.modifydate20180104081001-
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약학대학 > 약학과 > Journal papers
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