'''Structure of Thermoplasma acidophilum aldohexose dehydrogenase (AldT) in ligand-free form'''
===Structure of Thermoplasma acidophilum aldohexose dehydrogenase (AldT) in ligand-free form===
==Overview==
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The D-aldohexose dehydrogenase from the thermoacidophilic archaea Thermoplasma acidophilum (AldT) belongs to the short-chain dehydrogenase/reductase (SDR) superfamily and catalyzes the oxidation of several monosaccharides with a preference for NAD(+) rather than NADP(+) as a cofactor. It has been found that AldT is a unique enzyme that exhibits the highest dehydrogenase activity against D-mannose. Here, we describe the crystal structures of AldT in ligand-free form, in complex with NADH, and in complex with the substrate D-mannose, at 2.1 A, 1.65 A, and 1.6 A resolution, respectively. The AldT subunit forms a typical SDR fold with an unexpectedly long C-terminal tail and assembles into an intertwined tetramer. The D-mannose complex structure reveals that Glu84 interacts with the axial C2 hydroxyl group of the bound D-mannose. Structural comparison with Bacillus megaterium glucose dehydrogenase (BmGlcDH) suggests that the conformation of the glutamate side-chain is crucial for discrimination between D-mannose and its C2 epimer D-glucose, and the conformation of the glutamate side-chain depends on the spatial arrangement of nearby hydrophobic residues that do not directly interact with the substrate. Elucidation of the D-mannose recognition mechanism of AldT further provides structural insights into the unique substrate selectivity of AldT. Finally, we show that the extended C-terminal tail completely shuts the substrate-binding pocket of the neighboring subunit both in the presence and absence of substrate. The elaborate inter-subunit interactions between the C-terminal tail and the entrance of the substrate-binding pocket imply that the tail may play a pivotal role in the enzyme activity.
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==About this Structure==
==About this Structure==
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[[Category: Yasutake, Y.]]
[[Category: Yasutake, Y.]]
[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
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Revision as of 15:48, 29 July 2008
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Structure of Thermoplasma acidophilum aldohexose dehydrogenase (AldT) in ligand-free formStructure of Thermoplasma acidophilum aldohexose dehydrogenase (AldT) in ligand-free form
Structural insights into unique substrate selectivity of Thermoplasma acidophilum D-aldohexose dehydrogenase., Yasutake Y, Nishiya Y, Tamura N, Tamura T, J Mol Biol. 2007 Apr 6;367(4):1034-46. Epub 2007 Jan 16. PMID:17300803
