An integrated transport mechanism of the maltose ABC importer

Mächtel, Rebecca; Narducci, Alessandra; Griffith, Douglas A.; Cordes, Thorben and Orelle, Cédric (November 2019): An integrated transport mechanism of the maltose ABC importer. In: Research in microbiology, Vol. 170, No. 8: pp. 321-337

Abstract

ATP-binding cassette (ABC) transporters use the energy of ATP hydrolysis to transport a large diversity of molecules actively across biological membranes. A combination of biochemical, biophysical, and structural studies has established the maltose transporter MalFGK2 as one of the best characterized proteins of the ABC family. MalF and MalG are the transmembrane domains, and two MalKs form a homodimer of nucleotide-binding domains. A periplasmic maltose-binding protein (MalE) delivers maltose and other maltodextrins to the transporter, and triggers its ATPase activity. Substrate import occurs in a unidirectional manner by ATP-driven conformational changes in MalK2 that allow alternating access of the substrate-binding site in MalF to each side of the membrane. In this review, we present an integrated molecular mechanism of the transport process considering all currently available information. Furthermore, we summarize remaining inconsistencies and outline possible future routes to decipher the full mechanistic details of transport by MalEFGK2 complex and that of related importer systems.

• Item Type: Journal article
• EU Funded Grant Agreement Number: 638536
• EU Projects: Horizon 2020 > ERC Grants > ERC Starting Grant > ERC Grant 638536: SM-IMPORT - Substrate import at work: single-molecule studies of ABC transporters
• Faculties: Biology > Department Biology I
• Subjects: 500 Science > 570 Life sciences; biology
• Language: English