3RX9
3D structure of SciN from an Escherichia coli Patotype
Summary for 3RX9
Entry DOI | 10.2210/pdb3rx9/pdb |
Descriptor | Putative uncharacterized protein, SULFATE ION (3 entities in total) |
Functional Keywords | transthyretin (1sn5) fold, lipoprotein, t6ss assembly, scis, lipid binding protein |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 17071.32 |
Authors | Felisberto-Rodrigues, C.,Durand, E.,Aschtgen, M.-S.,Blangy, S.,Ortiz-Lombardia, M.,Douzy, B.,Cambillau, C.,Cascales, E. (deposition date: 2011-05-10, release date: 2011-12-07, Last modification date: 2024-04-03) |
Primary citation | Felisberto-Rodrigues, C.,Durand, E.,Aschtgen, M.S.,Blangy, S.,Ortiz-Lombardia, M.,Douzi, B.,Cambillau, C.,Cascales, E. Towards a Structural Comprehension of Bacterial Type VI Secretion Systems: Characterization of the TssJ-TssM Complex of an Escherichia coli Pathovar. Plos Pathog., 7:e1002386-e1002386, 2011 Cited by PubMed Abstract: Type VI secretion systems (T6SS) are trans-envelope machines dedicated to the secretion of virulence factors into eukaryotic or prokaryotic cells, therefore required for pathogenesis and/or for competition towards neighboring bacteria. The T6SS apparatus resembles the injection device of bacteriophage T4, and is anchored to the cell envelope through a membrane complex. This membrane complex is composed of the TssL, TssM and TagL inner membrane anchored proteins and of the TssJ outer membrane lipoprotein. Here, we report the crystal structure of the enteroaggregative Escherichia coli Sci1 TssJ lipoprotein, a two four-stranded β-sheets protein that exhibits a transthyretin fold with an additional α-helical domain and a protruding loop. We showed that TssJ contacts TssM through this loop since a loop depleted mutant failed to interact with TssM in vitro or in vivo. Biophysical analysis of TssM and TssJ-TssM interaction suggest a structural model of the membrane-anchored outer shell of T6SS. Collectively, our results provide an improved understanding of T6SS assembly and encourage structure-aided drug design of novel antimicrobials targeting T6SS. PubMed: 22102820DOI: 10.1371/journal.ppat.1002386 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
Download full validation report