The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold

@article{Ouyang1997TheFS,
  title={The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold},
  author={Songying Ouyang and Yuh-Ju Sun and John S. Rose and Yong-Je Chung and C. Hsiao and Wen-rui Chang and Ingrid Kuo and John Perozich and Ronald Lindahl and John Hempel and Bi-Cheng Wang},
  journal={Nature Structural Biology},
  year={1997},
  volume={4},
  pages={317-326}
}
The first structure of an aldehyde dehydrogenase (ALDH) is described at 2.6 Å resolution. Each subunit of the dimeric enzyme contains an NAD-binding domain, a catalytic domain and a bridging domain. At the interface of these domains is a 15 Å long funnel-shaped passage with a 6 × 12 Å opening leading to a putative catalytic pocket. A new mode of NAD binding, which differs substantially from the classic β-α-β binding mode associated with the ‘Rossmann fold’, is observed which we term the… CONTINUE READING

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