Crystal structure of thermostable acetaldehyde dehydrogenase from the hyperthermophilic archaeon, Sulfolobus tokodaii
Shohei Mine, Makoto Nakabayashi and Kazuhiko Ishikawa [1]
Molecular Tour
Aldehyde dehydrogenase (ALDH) plays an important role in aldehyde detoxification. Acetaldehyde is also considered carcinogenic and toxic. Thermostable ALDH from the hyperthermophilic archaeon Sulfolobus tokodaii (ALDHSt), exhibits high activity toward acetaldehyde and has potential applications as a biosensor for acetaldehyde. This structural information provides clues regarding the mechanisms of substrate recognition and thermostability in ALDH.
is a dimer of dimers (A/B and C/D) with crystallographic 222 symmetry. . The cofactor-binding domain, catalytic domain and oligomerization domain are shown in green, cyan and magenta, respectively. NADP is shown as a yellow stick model.
. NADP and NADP-interacting residues are shown in ball-and-stick representation, water molecules are shown as red spheres. Hydrogen bonds are shown as dashed lines. in ALDHSt are colored in deep pink.
References
- ↑ Mine S, Nakabayashi M, Ishikawa K. Crystal structure of thermostable acetaldehyde dehydrogenase from the hyperthermophilic archaeon Sulfolobus tokodaii. Acta Crystallogr F Struct Biol Commun. 2023 Jun 1;79(Pt 6):159-165. PMID:37227376 doi:10.1107/S2053230X23004430
