Assembling the tat protein translocase
| Autor: | Mark I. Wallace, Hajra Basit, Phillip J. Stansfeld, Johann Habersetzer, Matthew A. B. Baker, Felicity Alcock, Tracy Palmer, Ben C. Berks |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular 0301 basic medicine Receptor complex QH301-705.5 Science Plasma protein binding twin-arginine Molecular Dynamics Simulation Models Biological Biochemistry General Biochemistry Genetics and Molecular Biology Tat protein transport Twin-arginine translocation pathway 03 medical and health sciences Escherichia coli Translocase membrane protein Biology (General) General Immunology and Microbiology biology Membrane transport protein Escherichia coli Proteins General Neuroscience E. coli Membrane Transport Proteins General Medicine sequence co-evolution Biophysics and Structural Biology Transmembrane domain 030104 developmental biology Structural biology Membrane protein Biophysics biology.protein Medicine Protein Multimerization Protein Binding Research Article |
| Zdroj: | eLife, Vol 5 (2016) Wallace, M I, Alcock, F, Stansfeld, P J, Basit, H, Berks, B C, Habersetzer, J, Baker, M A B & Palmer, T 2016, ' Assembling the Tat protein translocase ', eLife . https://doi.org/10.7554/eLife.20718 eLife |
| ISSN: | 2050-084X |
| Popis: | The twin-arginine protein translocation system (Tat) transports folded proteins across the bacterial cytoplasmic membrane and the thylakoid membranes of plant chloroplasts. The Tat transporter is assembled from multiple copies of the membrane proteins TatA, TatB, and TatC. We combine sequence co-evolution analysis, molecular simulations, and experimentation to define the interactions between the Tat proteins of Escherichia coli at molecular-level resolution. In the TatBC receptor complex the transmembrane helix of each TatB molecule is sandwiched between two TatC molecules, with one of the inter-subunit interfaces incorporating a functionally important cluster of interacting polar residues. Unexpectedly, we find that TatA also associates with TatC at the polar cluster site. Our data provide a structural model for assembly of the active Tat translocase in which substrate binding triggers replacement of TatB by TatA at the polar cluster site. Our work demonstrates the power of co-evolution analysis to predict protein interfaces in multi-subunit complexes. DOI: http://dx.doi.org/10.7554/eLife.20718.001 |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|