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1kv9
From Proteopedia
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Structure at 1.9 A Resolution of a Quinohemoprotein Alcohol Dehydrogenase from Pseudomonas putida HK5
Overview
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 Structure
1KV9 is a Single protein structure of sequence from Pseudomonas putida with , , , , and as ligands. Full crystallographic information is available from OCA.
Reference
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 Thu Feb 21 13:38:15 2008
Categories: Pseudomonas putida | Single protein | Adachi, O. | Bellamy, H D. | Chen, Z W. | Fujii, T. | Mathews, F S. | Matsushita, K. | Toyama, H. | Yamashita, T. | ACN | CA | EPE | GOL | HEM | PQQ | Electron transfer | Quinohemoprotein alcohol dehydrogenase
