Crystallization and preliminary X-ray diffraction analysis of monkey dimeric dihydrodiol dehydrogenase.
Dihydrodiol dehydrogenase catalyzes the NADP(+)-linked oxidation of trans-dihydrodiols of aromatic hydrocarbons to corresponding catechols and exists in multiple forms in mammalian tissues. The dimeric form of mammalian dihydrodiol dehydrogenase has a primary structure distinct from the previously known mammalian enzymes and may constitute a novel protein family with the prokaryotic proteins. Monkey kidney dimeric dihydrodiol dehydrogenase was crystallized from buffered ammonium phosphate solution using the hanging-drop vapour-diffusion method. The crystals diffract to 2.65 A resolution in the laboratory and belong to the hexagonal P6(1)22 or P6(5)22 space group, with unit-cell parameters a = b = 122.8, c = 121.3 A, alpha = beta = 90, gamma = 120 degrees.
El-Kabbani
Ossama
O
Department of Medicinal Chemistry, Victorian College of Pharmacy, Monash University (Parkville Campus), Parkville, Victoria 3052, Australia. ossama.el-kabbani@vcp.monash.edu.au
Chung
Roland P T
RP
Ramsland
Paul A
PA
Asada
Yukuhiko
Y
Ishikura
Syuhei
S
Usami
Noriyuki
N
Hara
Akira
A
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D008251:Macaca; D010088:Oxidoreductases / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D011994:Recombinant Proteins; D010088:Oxidoreductases; C048338:trans-1,2-dihydrobenzene-1,2-diol dehydrogenase