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The twin-arginine translocation (Tat) pathway is one of two general protein transport systems found in the prokaryotic cytoplasmic membrane and is conserved in the thylakoid membrane of plant chloroplasts. The defining, and highly unusual, property of the Tat pathway is that it transports folded proteins, a task that must be achieved without allowing appreciable ion leakage across the membrane. The integral membrane TatC protein is the central component of the Tat pathway. TatC captures substrate proteins by binding their signal peptides. TatC then recruits TatA family proteins to form the active translocation complex. Here we report the crystal structure of TatC from the hyperthermophilic bacterium Aquifex aeolicus. This structure provides a molecular description of the core of the Tat translocation system and a framework for understanding the unique Tat transport mechanism.

Original publication

DOI

10.1038/nature11683

Type

Journal article

Journal

Nature

Publication Date

13/12/2012

Volume

492

Pages

210 - 214

Keywords

Binding Sites, Escherichia coli, Gram-Negative Bacteria, Membrane Transport Proteins, Models, Molecular, Protein Binding, Protein Sorting Signals, Protein Structure, Tertiary, Recombinant Proteins