Journal
NATURE
Volume 492, Issue 7428, Pages 210-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature11683
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Funding
- Wellcome Trust [083599, 092970MA]
- Swedish Foundation for Strategic Research
- Swedish Research Council [2010-5061]
- E.P. Abrahams Cephalosporin Trust
- Biotechnology and Biological Sciences Research Council [BB/E023347/1, BB/1019855/1]
- Medical Research Council [G1001640, G0900888]
- European Research Council
- James Martin 21st Century School Vaccine Design Institute
- BBSRC [BB/F02150X/1, BB/I019855/1, BB/H000267/1, BB/E023347/1] Funding Source: UKRI
- MRC [G1001640] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/I019855/1, BB/E023347/1, BB/H000267/1, BB/F02150X/1, BEP17032, BBS/B/16011, B19456] Funding Source: researchfish
- Medical Research Council [G1001640] Funding Source: researchfish
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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.
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