Structural and functional diversity calls for a new classification of ABC transporters.
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ABSTRACT:
SUBMITTER: Thomas C
PROVIDER: S-EPMC8386196 | biostudies-literature | 2020 Dec
REPOSITORIES: biostudies-literature
Publications
Structural and functional diversity calls for a new classification of ABC transporters.
Thomas Christoph C Aller Stephen G SG Beis Konstantinos K Carpenter Elisabeth P EP Chang Geoffrey G Chen Lei L Dassa Elie E Dean Michael M Duong Van Hoa Franck F Ekiert Damian D Ford Robert R Gaudet Rachelle R Gong Xin X Holland I Barry IB Huang Yihua Y Kahne Daniel K DK Kato Hiroaki H Koronakis Vassilis V Koth Christopher M CM Lee Youngsook Y Lewinson Oded O Lill Roland R Martinoia Enrico E Murakami Satoshi S Pinkett Heather W HW Poolman Bert B Rosenbaum Daniel D Sarkadi Balazs B Schmitt Lutz L Schneider Erwin E Shi Yigong Y Shyng Show-Ling SL Slotboom Dirk J DJ Tajkhorshid Emad E Tieleman D Peter DP Ueda Kazumitsu K Váradi András A Wen Po-Chao PC Yan Nieng N Zhang Peng P Zheng Hongjin H Zimmer Jochen J Tampé Robert R
FEBS letters 20201026 23
Members of the ATP-binding cassette (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 transmembrane domains (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 ...[more]
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