Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5.
The type II quinohemoprotein alcohol dehydrogenase of Pseudomonas putida is a periplasmic enzyme that oxidizes substrate alcohols to the aldehyde and transfers electrons first to pyrroloquinoline quinone (PQQ) and then to an internal heme group. The 1.9 A resolution crystal structure reveals that the enzyme contains a large N-terminal eight-stranded beta propeller domain (approximately 60 kDa) similar to methanol dehydrogenase and a small C-terminal c-type cytochrome domain (approximately 10 kDa) similar to the cytochrome subunit of p-cresol methylhydoxylase. The PQQ is bound near the axis of the propeller domain about 14 A from the heme. A molecule of acetone, the product of the oxidation of isopropanol present during crystallization, appears to be bound in the active site cavity.
Chen
Zhi-wei
ZW
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA.
Matsushita
Kazunobu
K
Yamashita
Tetsuo
T
Fujii
Taka-aki
TA
Toyama
Hirohide
H
Adachi
Osao
O
Bellamy
Henry D
HD
Mathews
F Scott
FS
D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D001400:Azurin / Q000378:metabolism; D020134:Catalytic Domain; D042843:Glucose 1-Dehydrogenase; D005948:Glucose Dehydrogenases / Q000378:metabolism; D008024:Ligands; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D017434:Protein Structure, Tertiary; D016958:Pseudomonas putida / Q000737:chemistry* / Q000378:metabolism; D016415:Sequence Alignment
D008024:Ligands; D001400:Azurin; D000429:Alcohol Oxidoreductases; D005948:Glucose Dehydrogenases; D042843:Glucose 1-Dehydrogenase; C019641:alcohol dehydrogenase (acceptor)