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Title 

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

Authors 

Eui-jeon WooS I RyuHyung Nam SongTaeYang JungS M YeonH A LeeByoung Chul ParkK H ParkS B Lee

Publisher 

Elsevier

Issue Date 

2010

Citation 

Journal of Molecular Biology, vol. 404, no. 2, pp. 247-259

Keywords 

GlycosyltransferasePyrococcus horikoshiiTrehalose synthaseTreTX-ray structure

Abstract 

Many 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 ? 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.

ISSN 

0022-2836

Link 

http://dx.doi.org/10.1016/j.jmb.2010.09.056

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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