1kv9
|
Structure at 1.9 A Resolution of a Quinohemoprotein Alcohol Dehydrogenase from Pseudomonas putida HK5
OverviewOverview
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.
About this StructureAbout this Structure
1KV9 is a Single protein structure of sequence from Pseudomonas putida with CA, PQQ, HEM, EPE, ACN and GOL as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5., Chen ZW, Matsushita K, Yamashita T, Fujii TA, Toyama H, Adachi O, Bellamy HD, Mathews FS, Structure. 2002 Jun;10(6):837-49. PMID:12057198
Page seeded by OCA on Sun Nov 25 02:00:30 2007