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Crystallization and preliminary X-ray diffraction analysis of monkey dimeric dihydrodiol dehydrogenase. | LitMetric

Crystallization and preliminary X-ray diffraction analysis of monkey dimeric dihydrodiol dehydrogenase.

Acta Crystallogr D Biol Crystallogr

Department of Medicinal Chemistry, Victorian College of Pharmacy, Monash University (Parkville Campus), Parkville, Victoria 3052, Australia.

Published: January 2002

AI Article Synopsis

  • Dihydrodiol dehydrogenase is an enzyme that oxidizes trans-dihydrodiols of aromatic hydrocarbons to catechols and has various forms in mammalian tissues.
  • The dimeric form of this enzyme has a unique structure that suggests it may be part of a new protein family related to prokaryotic enzymes.
  • The monkey kidney version of this enzyme has been crystallized, showing high-resolution diffraction, and its crystals belong to specific hexagonal space groups with defined unit-cell parameters.

Article Abstract

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.

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Source
http://dx.doi.org/10.1107/s090744490101811xDOI Listing

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