1KV9

Structure at 1.9 A Resolution of a Quinohemoprotein Alcohol Dehydrogenase from Pseudomonas putida HK5

Summary for 1KV9

• Entry DOI: 10.2210/pdb1kv9/pdb
• Related: 4AAH
• Descriptor: TYPE II QUINOHEMOPROTEIN ALCOHOL DEHYDROGENASE, CALCIUM ION, PYRROLOQUINOLINE QUINONE, ... (8 entities in total)
• Functional Keywords: quinohemoprotein alcohol dehydrogenase, electron transfer, oxidoreductase
• Biological source: Pseudomonas putida
• Total number of polymer chains: 1
• Total formula weight: 74086.27

Authors

Chen, Z.-W.,Matsushita, K.,Yamashita, T.,Fujii, T.,Toyama, H.,Adachi, O.,Bellamy, H.D.,Mathews, F.S. (deposition date: 2002-01-25, release date: 2002-07-10, Last modification date: 2024-11-06)

Primary citation

Chen, Z.W.,Matsushita, K.,Yamashita, T.,Fujii, T.A.,Toyama, H.,Adachi, O.,Bellamy, H.D.,Mathews, F.S.
Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5.
Structure, 10:837-849, 2002

PubMed Abstract: 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.

PubMed: 12057198
DOI: 10.1016/S0969-2126(02)00774-8

Experimental method

X-RAY DIFFRACTION (1.9 Å)