2XA2

Crystal structure of trehalose synthase TreT mutant E326A from P. horikoshii in complex with UDPG

Summary for 2XA2

• Entry DOI: 10.2210/pdb2xa2/pdb
• Related: 2XA2 2XA9
• Descriptor: TREHALOSE-SYNTHASE TRET, URIDINE-5'-DIPHOSPHATE-GLUCOSE (3 entities in total)
• Functional Keywords: biosynthetic protein
• Biological source: PYROCOCCUS HORIKOSHII
• Total number of polymer chains: 2
• Total formula weight: 97491.64

Authors

Song, H.-N.,Jung, T.-Y.,Yoon, S.-M.,Lee, S.-B.,Lim, M.-Y.,Woo, E.-J. (deposition date: 2010-03-26, release date: 2011-03-16, Last modification date: 2024-05-08)

Primary citation

Woo, E.-J.,Ryu, S.,Song, H.-N.,Jung, T.-Y.,Yeon, S.,Lee, H.,Park, B.C.,Park, K.,Lee, S.-B.
Structural Insights on the New Mechanism of Trehalose Synthesis by Trehalose Synthase Tret from Pyrococcus Horikoshii.
J.Mol.Biol., 404:247-, 2010

PubMed 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 Å 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.

PubMed: 20888836
DOI: 10.1016/J.JMB.2010.09.056

Experimental method

X-RAY DIFFRACTION (2.5 Å)