Document Detail

Structure of the TatC core of the twin-arginine protein transport system.
MedLine Citation:
PMID:  23201679     Owner:  NLM     Status:  MEDLINE    
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.
Sarah E Rollauer; Michael J Tarry; James E Graham; Mari Jääskeläinen; Franziska Jäger; Steven Johnson; Martin Krehenbrink; Sai-Man Liu; Michael J Lukey; Julien Marcoux; Melanie A McDowell; Fernanda Rodriguez; Pietro Roversi; Phillip J Stansfeld; Carol V Robinson; Mark S P Sansom; Tracy Palmer; Martin Högbom; Ben C Berks; Susan M Lea
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-12-02
Journal Detail:
Title:  Nature     Volume:  492     ISSN:  1476-4687     ISO Abbreviation:  Nature     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-12-13     Completed Date:  2012-12-21     Revised Date:  2014-07-31    
Medline Journal Info:
Nlm Unique ID:  0410462     Medline TA:  Nature     Country:  England    
Other Details:
Languages:  eng     Pagination:  210-4     Citation Subset:  IM    
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MeSH Terms
Binding Sites
Escherichia coli / genetics
Gram-Negative Bacteria / chemistry*,  genetics,  metabolism*
Membrane Transport Proteins / chemistry*,  metabolism
Models, Molecular*
Protein Binding
Protein Sorting Signals
Protein Structure, Tertiary
Recombinant Proteins / chemistry,  genetics
Grant Support
083599//Wellcome Trust; 083599//Wellcome Trust; 088150//Wellcome Trust; 092970//Wellcome Trust; 092970MA//Wellcome Trust; BB/1019855/1//Biotechnology and Biological Sciences Research Council; BB/E023347/1//Biotechnology and Biological Sciences Research Council; BB/I019855/1//Biotechnology and Biological Sciences Research Council; G0900888//Medical Research Council; G0900888(92020)//Medical Research Council; G100164//Medical Research Council; G1001640/1//Medical Research Council
Reg. No./Substance:
0/Membrane Transport Proteins; 0/Protein Sorting Signals; 0/Recombinant Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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