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This book provides a molecular view of membrane transport by means of numerous biochemical and biophysical techniques. The rapidly growing numbers of atomic structures of transporters in different conformations and the constant progress in bioinformatics have recently added deeper insights. The unifying mechanism of energized solute transport across membranes is assumed to consist of the conformational cycling of a carrier protein to provide access to substrate binding sites from either side of a cellular membrane. Due to the central role of active membrane transport there is considerable interest in deciphering the principles of one of the most fundamental processes in nature: the alternating access mechanism. This book brings together particularly significant structure-function studies on a variety of carrier systems from different transporter families: Glutamate symporters, LeuT-like fold transporters, MFS transporters and SMR (RND) exporters, as well as ABC-type importers. The selected examples impressively demonstrate how the combination of functional analysis, crystallography, investigation of dynamics and computational studies has made it possible to create a conclusive picture or more precisely, "a molecular movie". Although we are still far from a complete molecular description of the alternating access mechanism, remarkable progress has been made from static snapshots towards membrane transport dynamics.
Table des matières
Dance Lessons for Proteins: The Dynamics and Thermodynamics of a Sodium/Aspartate Symporter.- Characterizing the Structure, Function and Evolution of Human Solute Carrier (SLC) Transporters Using Computational Approaches.- Structures of the Prokaryotic Galactose Transporter vSGLT and Their Implications on Alternating Access Mechanism in Human SGLT1.- Moving Crystallographic Snapshots: A Mechanism for Transport Regulation in BetP.- Development of Refined Homology Models: Adding the Missing Information to the Medically Relevant Neurotransmitter Transporters.- The Life and Times of Lac Permease: Crystals Ain't Enough.- Alternating Access Within the POT Family of Oligopeptide.- Proton Symporters.- The Maltose ABC Transporter: Where Structure Meets Function.- Cooperative Transport Mechanism and Proton-Coupling in the Multidrug Efflux Transporter Complex ArcAB-TolC.- What Can a Living Fossil Tell Us About Evolution and Mechanism of Ion-Coupled Transporters: The Story of Small Multidrug Transporters Symmetrically Asymmetric: EmrE Seen from the NMR Perspective.
A propos de l'auteur
Reinhard Krämer is chair in Biochemistry at Cologne University, Germany. After studying Biochemistry at the Universities of Tübingen and Munich, he obtained his Ph.D. from LMU Munich. He then spent 10 years at the Research Center Jülich (Institute of Biotechnology) and the University of Düsseldorf as an Associate Professor for Biochemistry before taking up his present position at Cologne University. During his scientific career, R. Krämer has focused on different aspects of membrane transport proteins, both in mitochondria and in prokaryotes, as well as on stress response in bacteria, in particular osmotic stress.
Dr. des. Christine Ziegler, Studienrätin am Domgymnasium Fulda
Résumé
This book provides a molecular view of membrane transport by means of numerous biochemical and biophysical techniques. The rapidly growing numbers of atomic structures of transporters in different conformations and the constant progress in bioinformatics have recently added deeper insights. The unifying mechanism of energized solute transport across membranes is assumed to consist of the conformational cycling of a carrier protein to provide access to substrate binding sites from either side of a cellular membrane. Due to the central role of active membrane transport there is considerable interest in deciphering the principles of one of the most fundamental processes in nature: the alternating access mechanism. This book brings together particularly significant structure-function studies on a variety of carrier systems from different transporter families: Glutamate symporters, LeuT-like fold transporters, MFS transporters and SMR (RND) exporters, as well as ABC-type importers. The selected examples impressively demonstrate how the combination of functional analysis, crystallography, investigation of dynamics and computational studies has made it possible to create a conclusive picture or more precisely, “a molecular movie”. Although we are still far from a complete molecular description of the alternating access mechanism, remarkable progress has been made from static snapshots towards membrane transport dynamics.
