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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1973 Aug;70(8):2439–2442. doi: 10.1073/pnas.70.8.2439

Structure of Liver Alcohol Dehydrogenase at 2.9-Å Resolution

Carl-Ivar Brändén *, Hans Eklund *, Bo Nordström *, Torne Boiwe *, Gustaf Söderlund *, Eila Zeppezauer *, Ingrid Ohlsson *, Åke Åkeson *
PMCID: PMC433752  PMID: 4365379

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+.

Keywords: crystallographic strucutre, zinc, coenzyme binding

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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