2X9C
Crystal structure of a soluble PrgI mutant from Salmonella Typhimurium
Summary for 2X9C
Entry DOI | 10.2210/pdb2x9c/pdb |
Related | 2KV7 |
Descriptor | PROTEIN PRGI (2 entities in total) |
Functional Keywords | needle protomer, protein transport, bacterial pathogenesis |
Biological source | SALMONELLA TYPHIMURIUM |
Total number of polymer chains | 2 |
Total formula weight | 18182.07 |
Authors | Poyraz, O.,Schmidt, H.,Seidel, K.,Delissen, F.,Ader, C.,Tenenboim, H.,Goosmann, C.,Laube, B.,Thuenemann, A.F.,Zychlinsky, A.,Baldus, M.,Lange, A.,Griesinger, C.,Kolbe, M. (deposition date: 2010-03-15, release date: 2010-06-16, Last modification date: 2023-12-20) |
Primary citation | Poyraz, O.,Schmidt, H.,Seidel, K.,Delissen, F.,Ader, C.,Tenenboim, H.,Goosmann, C.,Laube, B.,Thuenemann, A.F.,Zychlinsky, A.,Baldus, M.,Lange, A.,Griesinger, C.,Kolbe, M. Protein Refolding is Required for Assembly of the Type Three Secretion Needle Nat.Struct.Mol.Biol., 17:788-, 2010 Cited by PubMed Abstract: Pathogenic Gram-negative bacteria use a type three secretion system (TTSS) to deliver virulence factors into host cells. Although the order in which proteins incorporate into the growing TTSS is well described, the underlying assembly mechanisms are still unclear. Here we show that the TTSS needle protomer refolds spontaneously to extend the needle from the distal end. We developed a functional mutant of the needle protomer from Shigella flexneri and Salmonella typhimurium to study its assembly in vitro. We show that the protomer partially refolds from alpha-helix into beta-strand conformation to form the TTSS needle. Reconstitution experiments show that needle growth does not require ATP. Thus, like the structurally related flagellar systems, the needle elongates by subunit polymerization at the distal end but requires protomer refolding. Our studies provide a starting point to understand the molecular assembly mechanisms and the structure of the TTSS at atomic level. PubMed: 20543831DOI: 10.1038/NSMB.1822 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.45 Å) |
Structure validation
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