Energy Coupling Efficiency in the Type I ABC Transporter GInPQ

被引:10
作者
Nijeholt, Jelger A. Lycklama A.
Vietrov, Ruslan
Schuurman-Wolters, Gea K.
Poolman, Bert [1 ]
机构
[1] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Dept Biochem, Nijenborgh 4, NL-9747 AG Groningen, Netherlands
关键词
SUBSTRATE-BINDING DOMAINS; PHOSPHOLIPID-BILAYER NANODISCS; MALTOSE TRANSPORTER; CONFORMATIONAL DYNAMICS; CASSETTE TRANSPORTER; LACTOCOCCUS-LACTIS; CRYSTAL-STRUCTURE; PERIPLASMIC LOOP; ATP HYDROLYSIS; PROTEIN;
D O I
10.1016/j.jmb.2018.02.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Solute transport via ATP binding cassette (ABC) importers involves receptor-mediated substrate binding, which is followed by ATP-driven translocation of the substrate across the membrane. How these steps are exactly initiated and coupled, and how much ATP it takes to complete a full transport cycle, are subject of debate. Here, we reconstitute the ABC importer GInPQ in nanodiscs and in proteoliposomes and determine substrate-(in)dependent ATP hydrolysis and transmembrane transport. We determined the conformational states of the substrate-binding domains (SBDs) by single-molecule Forster resonance energy transfer measurements. We find that the basal ATPase activity (ATP hydrolysis in the absence of substrate) is mainly caused by the docking of the closed-unliganded state of the SBDs onto the transporter domain of GInPQ and that, unlike glutamine, arginine binds both SBDs but does not trigger their closing. Furthermore, comparison of the ATPase activity in nanodiscs with glutamine transport in proteoliposomes shows that the stoichiometry of ATP per substrate is close to two. These findings help understand the mechanism of transport and the energy coupling efficiency in ABC transporters with covalently linked SBDs, which may aid our understanding of Type I ABC importers in general. (C) 2018 Elsevier Ltd. All rights reserved.
引用
收藏
页码:853 / 866
页数:14
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