Structural insights on the new mechanism of trehalose synthesis by trehalose synthase TreT from Pyrococcus horikoshii

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dc.contributor.authorEui-jeon Woo-
dc.contributor.authorS I Ryu-
dc.contributor.authorHyung Nam Song-
dc.contributor.authorTaeYang Jung-
dc.contributor.authorS M Yeon-
dc.contributor.authorH A Lee-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorK H Park-
dc.contributor.authorS B Lee-
dc.date.accessioned2017-04-19T09:20:16Z-
dc.date.available2017-04-19T09:20:16Z-
dc.date.issued2010-
dc.identifier.issn0022-2836-
dc.identifier.uri10.1016/j.jmb.2010.09.056ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9831-
dc.description.abstractMany microorganisms produce trehalose for stability and survival against various environmental stresses. Unlike the widely distributed trehalose-biosynthetic pathway, which utilizes uridine diphosphate glucose and glucose-6-phosphate, the newly identified enzyme trehalose glycosyltransferring synthase (TreT) from hyperthermophilic bacteria and archaea synthesizes an α,α-trehalose from nucleoside diphosphate glucose and glucose. In the present study, we determined the crystal structure of TreT from Pyrococcus horikoshii at 2.3 A resolution to understand the detailed mechanism of this novel trehalose synthase. The conservation of essential residues in TreT and the high overall structural similarity of the N-terminal domain to that of trehalose phosphate synthase (TPS) imply that the catalytic reaction of TreT for trehalose synthesis would follow a similar mechanism to that of TPS. The acceptor binding site of TreT shows a wide and commodious groove and lacks the long flexible loop that plays a gating role in ligand binding in TPS. The observation of a wide space at the fissure between two domains and the relative shift of the N-domain in one of the crystal forms suggest that an interactive conformational change between two domains would occur, allowing a more compact architecture for catalysis. The structural analysis and biochemical data in this study provide a molecular basis for understanding the synthetic mechanism of trehalose, or the nucleotide sugar in reverse reaction of the TreT, in extremophiles that may have important industrial implications.-
dc.publisherElsevier-
dc.titleStructural insights on the new mechanism of trehalose synthesis by trehalose synthase TreT from Pyrococcus horikoshii-
dc.title.alternativeStructural insights on the new mechanism of trehalose synthesis by trehalose synthase TreT from Pyrococcus horikoshii-
dc.typeArticle-
dc.citation.titleJournal of Molecular Biology-
dc.citation.number2-
dc.citation.endPage259-
dc.citation.startPage247-
dc.citation.volume404-
dc.contributor.affiliatedAuthorEui-jeon Woo-
dc.contributor.affiliatedAuthorHyung Nam Song-
dc.contributor.affiliatedAuthorTaeYang Jung-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.alternativeName우의전-
dc.contributor.alternativeName류수인-
dc.contributor.alternativeName송형남-
dc.contributor.alternativeName정태양-
dc.contributor.alternativeName윤세미-
dc.contributor.alternativeName이현아-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName박관화-
dc.contributor.alternativeName이수복-
dc.identifier.bibliographicCitationJournal of Molecular Biology, vol. 404, no. 2, pp. 247-259-
dc.identifier.doi10.1016/j.jmb.2010.09.056-
dc.subject.keywordGlycosyltransferase-
dc.subject.keywordPyrococcus horikoshii-
dc.subject.keywordTrehalose synthase-
dc.subject.keywordTreT-
dc.subject.keywordX-ray structure-
dc.subject.localGlycosyltransferase-
dc.subject.localglycosyltransferase-
dc.subject.localGlycosyltransferases-
dc.subject.localPyrococcus horikoshii-
dc.subject.localtrehalose synthase-
dc.subject.localTrehalose synthase-
dc.subject.localTreT-
dc.subject.localx-ray structure-
dc.subject.localX-ray structure-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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