The rocking bundle: a mechanism for ion-coupled solute flux by symmetrical transporters.
Crystal structures of the bacterial amino acid transporter LeuT have provided the basis for understanding the conformational changes associated with substrate translocation by a multitude of transport proteins with the same fold. Biochemical and modeling studies led to a "rocking bundle" mechanism for LeuT that was validated by subsequent transporter structures. These advances suggest how coupled solute transport might be defined by the internal symmetry of proteins containing inverted structural repeats.
Forrest
Lucy R
LR
Computational Structural Biology, Max Planck Institute for Biophysics, Frankfurt, Germany.
Rudnick
Gary
G
D001665:Binding Sites; D029968:Escherichia coli Proteins / Q000378:metabolism; D017136:Ion Transport / Q000502:physiology*; D007477:Ions / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000378:metabolism*; D011487:Protein Conformation
D029968:Escherichia coli Proteins; D007477:Ions; D026901:Membrane Transport Proteins