2L16
Solution structure of Bacillus subtilits TatAd protein in DPC micelles
Summary for 2L16
| Entry DOI | 10.2210/pdb2l16/pdb |
| Descriptor | Sec-independent protein translocase protein tatAd (1 entity in total) |
| Functional Keywords | membrane protein, protein transport |
| Biological source | Bacillus subtilis |
| Cellular location | Membrane; Single-pass membrane protein: O31467 |
| Total number of polymer chains | 1 |
| Total formula weight | 8510.84 |
| Authors | |
| Primary citation | Hu, Y.,Zhao, E.,Li, H.,Xia, B.,Jin, C. Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis J.Am.Chem.Soc., 132:15942-15944, 2010 Cited by PubMed Abstract: The twin-arginine transport (Tat) system translocates folded proteins across the bacterial cytoplasmic or chloroplast thylakoid membrane of plants. The Tat system in most Gram-positive bacteria consists of two essential components, the TatA and TatC proteins. TatA is considered to be a bifunctional subunit, which can form a protein-conducting channel by self-oligomerization and can also participate in substrate recognition. However, the molecular mechanism underlying protein translocation remains elusive. Herein, we report the solution structure of the TatA(d) protein from Bacillus subtilis by NMR spectroscopy, the first structure of the Tat system at atomic resolution. TatA(d) shows an L-shaped structure formed by a transmembrane helix and an amphipathic helix, while the C-terminal tail is largely unstructured. Our results strongly support the postulated topology of TatA(d) in which the transmembrane helix is inserted into the lipid bilayer while the amphipathic helix lies at the membrane-water interface. Moreover, the structure of TatA(d) revealed the structural importance of several conserved residues at the hinge region, thus shedding new light on further elucidation of the protein transport mechanism of the Tat system. PubMed: 20726548DOI: 10.1021/ja1053785 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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