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Structural biology

The ABC of a versatile engine

Nature volume 396, pages 623–624 (1998)Cite this article

Early in evolution an engine called a nucleotide-binding domain (NBD) was created. As evolution progressed, this engine proved quite adaptable — it now powers an amazing variety of machines. On page 703 of this issue, Hung and colleagues1 describe the structure of the histidine permease NBD domain from Salmonella typhimurium, giving us a first look at this remarkable molecular engine. And, like any engine seen for the first time, we are eager to find out how it works.

Members of a large family of proteins called the ATP-binding cassette (ABC) transporters2 contain two NBDs together with two membrane-spanning domains (MSDs). These proteins are found in archaea, eubacteria and eukaryotes, and are increasingly recognized as the cause of human genetic diseases. The NBDs of different ABC transporters have considerable sequence similarity, and they all bind and hydrolyse ATP. In contrast, the transmembrane helices in the MSDs show little sequence similarity.

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Figure 1: The nucleotide-binding domain (NBD) of Salmonella typhimurium.
Figure 2: ABC transporter proteins.

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Authors and Affiliations

  1. the University of Iowa College of Medicine, Iowa City, 52242, Iowa, USA

    Michael J. Welsh, Andrew D. Robertson & Lynda S. Ostedgaard

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  1. Michael J. Welsh
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  2. Andrew D. Robertson
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  3. Lynda S. Ostedgaard
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Welsh, M., Robertson, A. & Ostedgaard, L. The ABC of a versatile engine. Nature 396, 623–624 (1998). https://doi.org/10.1038/25234

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