6N38
Structure of the type VI secretion system TssK-TssF-TssG baseplate subcomplex revealed by cryo-electron microscopy - full map sharpened
Summary for 6N38
| Entry DOI | 10.2210/pdb6n38/pdb |
| EMDB information | 9341 9342 9343 |
| Descriptor | Putative type VI secretion protein, Unassigned protein, ... (4 entities in total) |
| Functional Keywords | type vi secretion system, enteroaggregative e. coli, protein secretion, baseplate, structural genomics, seattle structural genomics center for infectious disease, ssgcid, protein transport |
| Biological source | Escherichia coli O44:H18 (strain 042 / EAEC) More |
| Total number of polymer chains | 11 |
| Total formula weight | 389978.64 |
| Authors | Park, Y.J.,Lacourse, K.D.,Cambillau, C.,Seattle Structural Genomics Center for Infectious Disease (SSGCID),DiMaio, F.,Mougous, J.D.,Veesler, D. (deposition date: 2018-11-14, release date: 2018-12-26, Last modification date: 2024-03-20) |
| Primary citation | Park, Y.J.,Lacourse, K.D.,Cambillau, C.,DiMaio, F.,Mougous, J.D.,Veesler, D. Structure of the type VI secretion system TssK-TssF-TssG baseplate subcomplex revealed by cryo-electron microscopy. Nat Commun, 9:5385-5385, 2018 Cited by PubMed Abstract: Type VI secretion systems (T6SSs) translocate effectors into target cells and are made of a contractile sheath and a tube docked onto a multi-protein transmembrane complex via a baseplate. Although some information is available about the mechanisms of tail contraction leading to effector delivery, the detailed architecture and function of the baseplate remain unknown. Here, we report the 3.7 Å resolution cryo-electron microscopy reconstruction of an enteroaggregative Escherichia coli baseplate subcomplex assembled from TssK, TssF and TssG. The structure reveals two TssK trimers interact with a locally pseudo-3-fold symmetrical complex comprising two copies of TssF and one copy of TssG. TssF and TssG are structurally related to each other and to components of the phage T4 baseplate and of the type IV secretion system, strengthening the evolutionary relationships among these macromolecular machines. These results, together with bacterial two-hybrid assays, provide a structural framework to understand the T6SS baseplate architecture. PubMed: 30568167DOI: 10.1038/s41467-018-07796-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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