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Structural insights into unique substrate selectivity of Thermoplasma acidophilum D-aldohexose dehydrogenase

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Title: Structural insights into unique substrate selectivity of Thermoplasma acidophilum D-aldohexose dehydrogenase
Authors: Yasutake, Yoshiaki Browse this author
Nishiya, Yoshiaki Browse this author
Tamura, Noriko Browse this author
Tamura, Tomohiro Browse this author →KAKEN DB
Keywords: D-aldohexose dehydrogenase
D-glucose dehydrogenase
D-mannose
short-chain dehydrogenase/reductase (SDR)
Thermoplasma acidophilum
Issue Date: 6-Apr-2007
Publisher: Elsevier
Journal Title: Journal of Molecular Biology
Volume: 367
Issue: 4
Start Page: 1034
End Page: 1046
Publisher DOI: 10.1016/j.jmb.2007.01.029
PMID: 17300803
Abstract: 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 Å, 1.65 Å, and 1.6 Å 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.
Relation: http://www.sciencedirect.com/science/journal/00222836
Type: article (author version)
URI: http://hdl.handle.net/2115/22096
Appears in Collections:農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 田村 具博

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