title: Structure and mechanism of energy-coupling factor transporters.
abstract: Energy-coupling factor (ECF) transporters form a new family of ATP-binding cassette (ABC) transporters and are widely used by prokaryotes to take up micronutrients from the environment. Instead of using the periplasmic solute-binding proteins (SBPs), ECF transporters use the membrane S proteins for substrate capture and translocation. In this review, we will focus on structural advances that have been made regarding how substrates are recognized by ECF transporters and possible transport mechanisms employed by the ECF transporters.
authors.affiliation: National Key Laboratory of Plant Molecular Genetics, CAS Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 300 Fenglin Road, Shanghai 200032, China. Electronic address: pengzhang01@sibs.ac.cn.
authors.forename: Peng
authors.initials: P
authors.lastname: Zhang
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001419:Bacteria / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular
chemical_list: D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins
keywords: ATP-binding cassette transporters; ECF fold; XRX motif; energy-coupling factor transporters; substrate specificity; transport mechanism