Structural diversity of ABC transporters

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300 Citaten (Scopus)
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Samenvatting

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.

Originele taal-2English
Pagina's (van-tot)419-435
Aantal pagina's17
TijdschriftJournal of general physiology
Volume143
Nummer van het tijdschrift4
DOI's
StatusPublished - apr.-2014

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