4B4A

Structure of the TatC core of the twin arginine protein translocation system

Summary for 4B4A

• Entry DOI: 10.2210/pdb4b4a/pdb
• Descriptor: SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC, Lauryl Maltose Neopentyl Glycol (2 entities in total)
• Functional Keywords: transport protein, tat secretion system, protein translocation
• Biological source: AQUIFEX AEOLICUS
• Cellular location: Cell inner membrane; Multi-pass membrane protein (By similarity): O67305
• Total number of polymer chains: 1
• Total formula weight: 29427.77

Authors

Rollauer, S.E.,Tarry, M.J.,Jaaskelainen, M.,Graham, J.E.,Jaeger, F.,Krehenbrink, M.,Roversi, P.,McDowell, M.A.,Stansfeld, P.J.,Johnson, S.,Liu, S.M.,Lukey, M.J.,Marcoux, J.,Robinson, C.V.,Sansom, M.S.,Palmer, T.,Hogbom, M.,Berks, B.C.,Lea, S.M. (deposition date: 2012-07-30, release date: 2012-12-05, Last modification date: 2024-11-13)

Primary citation

Rollauer, S.E.,Tarry, M.J.,Graham, J.E.,Jaaskelainen, M.,Jager, F.,Johnson, S.,Krehenbrink, M.,Liu, S.,Lukey, M.J.,Marcoux, J.,Mcdowell, M.A.,Rodriguez, F.,Roversi, P.,Stansfeld, P.J.,Robinson, C.V.,Sansom, M.S.P.,Palmer, T.,Hogbom, M.,Berks, B.C.,Lea, S.M.
Structure of the Tatc Core of the Twin-Arginine Protein Transport System.
Nature, 49:210-, 2012

PubMed Abstract: 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.

PubMed: 23201679
DOI: 10.1038/NATURE11683

Experimental method

X-RAY DIFFRACTION (3.5 Å)