Publication Date:
2012-12-04
Description:
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.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3573685/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3573685/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rollauer, Sarah E -- Tarry, Michael J -- Graham, James E -- Jaaskelainen, Mari -- Jager, Franziska -- Johnson, Steven -- Krehenbrink, Martin -- Liu, Sai-Man -- Lukey, Michael J -- Marcoux, Julien -- McDowell, Melanie A -- Rodriguez, Fernanda -- Roversi, Pietro -- Stansfeld, Phillip J -- Robinson, Carol V -- Sansom, Mark S P -- Palmer, Tracy -- Hogbom, Martin -- Berks, Ben C -- Lea, Susan M -- 083599/Wellcome Trust/United Kingdom -- 088150/Wellcome Trust/United Kingdom -- 092970/Wellcome Trust/United Kingdom -- 092970MA/Wellcome Trust/United Kingdom -- BB/1019855/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/E023347/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/F02150X/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/I019855/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- G0900888/Medical Research Council/United Kingdom -- G0900888(92020)/Medical Research Council/United Kingdom -- G100164/Medical Research Council/United Kingdom -- G1001640/Medical Research Council/United Kingdom -- G1001640/1/Medical Research Council/United Kingdom -- England -- Nature. 2012 Dec 13;492(7428):210-4. doi: 10.1038/nature11683. Epub 2012 Dec 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23201679" target="_blank"〉PubMed〈/a〉
Keywords:
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
Print ISSN:
0028-0836
Electronic ISSN:
1476-4687
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
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