Structural basis for TatA oligomerization: an NMR study of Escherichia coli TatA dimeric structure.

ABSTRACT: Many proteins are transported across lipid membranes by protein translocation systems in living cells. The twin-arginine transport (Tat) system identified in bacteria and plant chloroplasts is a unique system that transports proteins across membranes in their fully-folded states. Up to date, the detailed molecular mechanism of this process remains largely unclear. The Escherichia coli Tat system consists of three essential transmembrane proteins: TatA, TatB and TatC. Among them, TatB and TatC form a tight complex and function in substrate recognition. The major component TatA contains a single transmembrane helix followed by an amphipathic helix, and is suggested to form the translocation pore via self-oligomerization. Since the TatA oligomer has to accommodate substrate proteins of variou

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC4121141 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature