Structure of Liver Alcohol Dehydrogenase at 2.9-Å Resolution

Authors:
  • CBCarl-Ivar Brändén
    Carl-Ivar Brändén
  • HEHans Eklund
    Hans Eklund
  • BNBo Nordström
    Bo Nordström
  • TBTorne Boiwe
    Torne Boiwe
  • GSGustaf Söderlund
    Gustaf Söderlund
  • EZEila Zeppezauer
    Eila Zeppezauer
  • IOIngrid Ohlsson
    Ingrid Ohlsson
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Abstract
The conformation of the polypeptide chain in horse liver alcohol dehydrogenase (EC 1.1.1.1), as well as the binding sites for some inhibitor molecules, have been determined from x-ray crystallographic data to a resolution of 2.9 Å. Each subunit of the dimeric molecule is organized into two parts unequal in size and separated by a wide and deep active-site cleft. The adenosine moiety of the coenzyme is bound within the smaller region. Interactions between these coenzyme-binding substructures define the subunit contact area of the molecule. The “catalytic” zinc atoms are bound at the bottom of the clefts about 20 Å from the surface of the molecule. The coenzyme binding region has a main-chain conformation very similar to a corresponding region in lactate and malate dehydrogenase. It is suggested that this substructure is a general one for binding of nucleotides and, in particular, the coenzyme NAD + .

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