6CJD
NMR Structure of Salmonella Type III Secretion system protein OrgC
Summary for 6CJD
| Entry DOI | 10.2210/pdb6cjd/pdb |
| NMR Information | BMRB: 30417 |
| Descriptor | Putative cytoplasmic protein (1 entity in total) |
| Functional Keywords | controls needle assembly of t3ss, early substrate of t3ss, protein binding |
| Biological source | Salmonella enterica I |
| Total number of polymer chains | 1 |
| Total formula weight | 14293.89 |
| Authors | DEY, S.,DE GUZMAN, R.N. (deposition date: 2018-02-26, release date: 2018-08-01, Last modification date: 2024-05-15) |
| Primary citation | Kato, J.,Dey, S.,Soto, J.E.,Butan, C.,Wilkinson, M.C.,De Guzman, R.N.,Galan, J.E. A protein secreted by theSalmonellatype III secretion system controls needle filament assembly. Elife, 7:-, 2018 Cited by PubMed Abstract: Type III protein secretion systems (T3SS) are encoded by several pathogenic or symbiotic bacteria. The central component of this nanomachine is the needle complex. Here we show in a Typhimurium T3SS that assembly of the needle filament of this structure requires OrgC, a protein encoded within the T3SS gene cluster. Absence of OrgC results in significantly reduced number of needle substructures but does not affect needle length. We show that OrgC is secreted by the T3SS and that exogenous addition of OrgC can complement a mutation. We also show that OrgC interacts with the needle filament subunit PrgI and accelerates its polymerization into filaments in vitro. The structure of OrgC shows a novel fold with a shared topology with a domain from flagellar capping proteins. These findings identify a novel component of T3SS and provide new insight into the assembly of the type III secretion machine. PubMed: 30015613DOI: 10.7554/eLife.35886 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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