title: Thermodynamics of ABC transporters.
abstract: ABC transporters form the largest of all transporter families, and their structural study has made tremendous progress over recent years. However, despite such advances, the precise mechanisms that determine the energy-coupling between ATP hydrolysis and the conformational changes following substrate binding remain to be elucidated. Here, we present our thermodynamic analysis for both ABC importers and exporters, and introduce the two new concepts of differential-binding energy and elastic conformational energy into the discussion. We hope that the structural analysis of ABC transporters will henceforth take thermodynamic aspects of transport mechanisms into account as well.
authors.affiliation: National Laboratory of Macromolecules, National Center of Protein Science-Beijing, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China. zhangc@ibp.ac.cn.
authors.forename: Xuejun C
authors.initials: XC
authors.lastname: Zhang
authors.affiliation: National Laboratory of Macromolecules, National Center of Protein Science-Beijing, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
authors.forename: Lei
authors.initials: L
authors.lastname: Han
authors.affiliation: National Laboratory of Macromolecules, National Center of Protein Science-Beijing, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
authors.forename: Yan
authors.initials: Y
authors.lastname: Zhao
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000502:physiology*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D006801:Humans; D008962:Models, Theoretical; D013816:Thermodynamics
chemical_list: D018528:ATP-Binding Cassette Transporters; D000255:Adenosine Triphosphate
keywords: ABC transporters; differential-binding energy; elastic conformational energy; energy-coupling