4HTT
Crystal Structure of Twin Arginine Translocase Receptor- TatC in DDM
Summary for 4HTT
| Entry DOI | 10.2210/pdb4htt/pdb |
| Related | 4HTS |
| Descriptor | Sec-independent protein translocase protein TatC, Lysozyme (1 entity in total) |
| Functional Keywords | twin arginine translocase receptor, membrane, hydrolase |
| Biological source | Aquifex aeolicus VF5 More |
| Total number of polymer chains | 2 |
| Total formula weight | 94689.98 |
| Authors | Ramasamy, S.,Suloway, C.J.M.,Clemons Jr., W.M. (deposition date: 2012-11-01, release date: 2013-05-01, Last modification date: 2024-02-28) |
| Primary citation | Ramasamy, S.,Abrol, R.,Suloway, C.J.,Clemons, W.M. The Glove-like Structure of the Conserved Membrane Protein TatC Provides Insight into Signal Sequence Recognition in Twin-Arginine Translocation. Structure, 21:777-788, 2013 Cited by PubMed Abstract: In bacteria, two signal-sequence-dependent secretion pathways translocate proteins across the cytoplasmic membrane. Although the mechanism of the ubiquitous general secretory pathway is becoming well understood, that of the twin-arginine translocation pathway, responsible for translocation of folded proteins across the bilayer, is more mysterious. TatC, the largest and most conserved of three integral membrane components, provides the initial binding site of the signal sequence prior to pore assembly. Here, we present two crystal structures of TatC from the thermophilic bacteria Aquifex aeolicus at 4.0 Å and 6.8 Å resolution. The membrane architecture of TatC includes a glove-shaped structure with a lipid-exposed pocket predicted by molecular dynamics to distort the membrane. Correlating the biochemical literature to these results suggests that the signal sequence binds in this pocket, leading to structural changes that facilitate higher order assemblies. PubMed: 23583035DOI: 10.1016/j.str.2013.03.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (6.8 Å) |
Structure validation
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