Journal or Book Title
Journal of Bacteriology
SecA facilitates protein transport across the eubacterial plasma membrane by its association with cargo proteins and the SecYEG translocon, followed by ATP-driven conformational changes that promote protein translocation in a stepwise manner. Whether SecA functions as a monomer or a dimer during this process has been the subject of considerable controversy. Here we utilize cysteine-directed mutagenesis along with the crystal structure of the SecA dimer to create a cross-linked dimer at its subunit interface, which was normally active for in vitro protein translocation.
Oliver, Don, "SecA Dimer Cross-linked at its Subunit Interface is Functional for Protein Translocation" (2006). Division III Faculty Publications. 87.