PubReading [288] - Structural and functional diversity calls for a new classification of ABC transporters - C. Thomas, J. Zimmer and R. Tampe

<p>Members of the <strong>ATP-binding cassette</strong> (ABC) transporter superfamily translocate a broad spectrum of chemically diverse substrates. While their eponymous ATP-binding cassette in the nucleotide-binding domains (NBDs) is highly conserved, their <strong>transmembrane domains</strong> (TMDs) forming the translocation pathway exhibit distinct folds and topologies, suggesting that during evolution the ancient motor domains were combined with different transmembrane mechanical systems to orchestrate a variety of cellular processes. In recent years, it has become increasingly evident that the distinct TMD folds are best suited to categorize the multitude of <strong>ABC transporters</strong>. We therefore propose a new ABC transporter classification that is based on <strong>structural homology</strong> in the TMDs.</p><p><em>doi:10.1002/1873-3468.13935 - 2020</em></p>