title: Bacterial export takes its Tol.
abstract: The recent crystal structure of TolC elegantly indicates its function and provides insight into its mechanism for export of a wide range of molecules across the periplasmic space and outer membrane of Gram-negative bacteria. The structure is compared to those of other proteins that are embedded in bacterial outer membranes or that traverse the periplasmic space.
authors.affiliation: Department of Molecular Physiology and Biological Physics, University of Virginia, PO Box 800736, Charlottesville, VA 22908-0736, USA. mwiener@virginia.edu
authors.forename: M C
authors.initials: MC
authors.lastname: Wiener
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D029968:Escherichia coli Proteins; D006090:Gram-Negative Bacteria / Q000378:metabolism; D026901:Membrane Transport Proteins; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D021122:Protein Subunits
chemical_list: D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D021122:Protein Subunits; C073126:tolC protein, E coli