ABC transporters: A structure-function perspective

Research output: Chapter in Book/Report/Conference proceedingChapterAcademic

Abstract

Most ABC importers employ a soluble substrate-binding protein (SBP) to capture the ligand and donate the molecule to the translocator. The SBP can be a soluble periplasmic protein or tethered to the membrane via a lipid moiety or protein anchor or fused to the translocator. In the hybrid ABC transporters, multiple substrate-binding domains (SBDs) can be fused in tandem and provide several extracytoplasmic substrate-binding sites. The substrate is transferred from the SBP to the membrane domain, which translocates the substrate via alternating access of a membrane-embedded substrate-binding pocket. A subset of ABC transporters, known as the energy-coupling factor (ECF) transporters, employs a membrane-embedded S-component to capture the substrate. The S-component guided by the ECF module transports the substrate over the membrane via a so-called toppling mechanism. An overview of the mechanisms of transport by the different types of ABC importers is presented, together with structural information about the proteins.
Original languageEnglish
Title of host publicationABC Transporters - 40 Years on
EditorsAnthony M. George
PublisherSpringer Verlag
Pages3-36
Number of pages34
Volume1
Edition1
ISBN (Electronic)978-3-319-23476-2
ISBN (Print)978-3-319-23475-5
Publication statusPublished - 17-Dec-2015

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