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Structure of the TatC core of the twin-arginine protein transport system
Open accessAbstract
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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MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
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Celniker, G., Nimrod, G., Ashkenazy, H., Glaser, F., Martz, E., Mayrose, I., Pupko, T., & Ben‐Tal, N. (2013) · Israel Journal of Chemistry · doi:10.1002/ijch.201200096 · Cited by 560
A saposin-lipoprotein nanoparticle system for membrane proteins
Frauenfeld, J., Löving, R., Armache, J.-P., Sonnen, A. F.-P., Guettou, F., Moberg, P., Zhu, L., Jegerschöld, C., Flayhan, A., Briggs, J. A. G., et al. (2016) · Nature Methods · doi:10.1038/nmeth.3801 · Cited by 293
Kudva, R., Denks, K., Kuhn, P., Vogt, A., Müller, M., & Koch, H.-G. (2013) · Research in Microbiology · doi:10.1016/j.resmic.2013.03.016 · Cited by 177
Structural Symmetry in Membrane Proteins
Forrest, L. R. (2015) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-051013-023008 · Cited by 148
Metadata
- Authors
- Rollauer, S. E., Tarry, M. J., Graham, J. E., Jääskeläinen, M., Jäger, F., Johnson, S., Krehenbrink, M., Liu, S.-M., Lukey, M. J., Marcoux, J., McDowell, M. A., Rodriguez, F., Roversi, P., Stansfeld, P. J., Robinson, C. V., Sansom, M. S. P., Palmer, T., Högbom, M., Berks, B. C., & Lea, S. M.
- Venue
- Nature
- Published
- 2012-12
- Volume
- 492
- Issue
- 7428
- Pages
- 210-214
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2061775535
- Cited by
- 181
- References
- 1
- FWCI
- 10.27
- Type
- journal article
- Language
- en
- Open access
- green
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- Rollauer, S. E., Tarry, M. J., Graham, J. E., Jääskeläinen, M., Jäger, F., Johnson, S., Krehenbrink, M., Liu, S.-M., Lukey, M. J., Marcoux, J., McDowell, M. A., Rodriguez, F., Roversi, P., Stansfeld, P. J., Robinson, C. V., Sansom, M. S. P., Palmer, T., Högbom, M., Berks, B. C., & Lea, S. M. (2012). Structure of the TatC core of the twin-arginine protein transport system. Nature. https://doi.org/10.1038/nature11683
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