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  • Title: SecA dimer cross-linked at its subunit interface is functional for protein translocation.
    Author: Jilaveanu LB, Oliver D.
    Journal: J Bacteriol; 2006 Jan; 188(1):335-8. PubMed ID: 16352850.
    Abstract:
    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.
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