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Updated: May 2, 2026

A Step-by-step Method for the Reconstitution of an ABC Transporter into Nanodisc Lipid Particles
Published on: August 31, 2012
Structural diversity of ABC transporters
Josy ter Beek1, Albert Guskov, Dirk Jan Slotboom
1Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, Netherlands.
Abstract:
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.
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