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Structural diversity of ABC transporters

ter Beek, J., Guskov, A. & Slotboom, D. J., Apr-2014, In : Journal of general physiology. 143, 4, p. 419-435 17 p.

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DOI

ATP-binding cassette (ABC) transporters form a large superfamily of ATP-dependent protein complexes that mediate transport of a vast array of substrates across membranes. The 14 currently available structures of ABC transporters have greatly advanced insight into the transport mechanism and revealed a tremendous structural diversity. Whereas the domains that hydrolyze ATP are structurally related in all ABC transporters, the membrane-embedded domains, where the substrates are translocated, adopt four different unrelated folds. Here, we review the structural characteristics of ABC transporters and discuss the implications of this structural diversity for mechanistic diversity.

Original languageEnglish
Pages (from-to)419-435
Number of pages17
JournalJournal of general physiology
Volume143
Issue number4
Publication statusPublished - Apr-2014

    Keywords

  • BINDING CASSETTE TRANSPORTER, COUPLING FACTOR TRANSPORTER, INWARD-FACING CONFORMATION, ATP-BINDING, ESCHERICHIA-COLI, MALTOSE TRANSPORTER, CRYSTAL-STRUCTURE, P-GLYCOPROTEIN, ALTERNATING ACCESS, MEMBRANE-PROTEINS

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