Bipartite gating in the outer membrane protein FecA.
The recent structure determination of FecA, with and without ligand, shows the existence of two gates. These are the extracellular loops closing over the binding site and the plug located inside the barrel. It indicates a process which is described as bipartite gating and allows for a rational distinction between the binding event and the transport process.
van der Helm
D
D
Department of Chemistry and Biochemistry, University of Oklahoma, 620 Parrington Oval, Norman, OK 73019, USA. dvdhelm@chemdept.chem.ou.edu
Chakraborty
R
R
Ferguson
A D
AD
Smith
B S
BS
Esser
L
L
Deisenhofer
J
J
D001425:Bacterial Outer Membrane Proteins / Q000502:physiology*; D001692:Biological Transport; D002352:Carrier Proteins / Q000502:physiology*; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D011485:Protein Binding; D017433:Protein Structure, Secondary; D011956:Receptors, Cell Surface; D015398:Signal Transduction / Q000502:physiology
D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; C028589:FecA protein, E coli; D011956:Receptors, Cell Surface