title: Structure of the TatC core of the twin-arginine protein transport system.
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.
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
authors.forename: Sarah E
authors.initials: SE
authors.lastname: Rollauer
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Tarry
authors.forename: James E
authors.initials: JE
authors.lastname: Graham
authors.forename: Mari
authors.initials: M
authors.lastname: Jääskeläinen
authors.forename: Franziska
authors.initials: F
authors.lastname: Jäger
authors.forename: Steven
authors.initials: S
authors.lastname: Johnson
authors.forename: Martin
authors.initials: M
authors.lastname: Krehenbrink
authors.forename: Sai-Man
authors.initials: SM
authors.lastname: Liu
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Lukey
authors.forename: Julien
authors.initials: J
authors.lastname: Marcoux
authors.forename: Melanie A
authors.initials: MA
authors.lastname: McDowell
authors.forename: Fernanda
authors.initials: F
authors.lastname: Rodriguez
authors.forename: Pietro
authors.initials: P
authors.lastname: Roversi
authors.forename: Phillip J
authors.initials: PJ
authors.lastname: Stansfeld
authors.forename: Carol V
authors.initials: CV
authors.lastname: Robinson
authors.forename: Mark S P
authors.initials: MS
authors.lastname: Sansom
authors.forename: Tracy
authors.initials: T
authors.lastname: Palmer
authors.forename: Martin
authors.initials: M
authors.lastname: Högbom
authors.forename: Ben C
authors.initials: BC
authors.lastname: Berks
authors.forename: Susan M
authors.initials: SM
authors.lastname: Lea
mesh_terms: D001665:Binding Sites; D004926:Escherichia coli / Q000235:genetics; D006090:Gram-Negative Bacteria / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D021382:Protein Sorting Signals; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
chemical_list: D026901:Membrane Transport Proteins; D021382:Protein Sorting Signals; D011994:Recombinant Proteins