2KV7
NMR solution structure of a soluble PrgI mutant from Salmonella Typhimurium
Summary for 2KV7
Entry DOI | 10.2210/pdb2kv7/pdb |
NMR Information | BMRB: 16770 |
Descriptor | Protein prgI (1 entity in total) |
Functional Keywords | prgi, bacterial pathogenesis, type three secretion needle, protein transport, needle protomer, transport, virulence |
Biological source | Salmonella typhimurium |
Total number of polymer chains | 1 |
Total formula weight | 9091.04 |
Authors | Schmidt, H.,Poyraz, O.,Seidel, K.,Delissen, F.,Ader, C.,Tenenboim, H.,Goosmann, C.,Laube, B.,Thuenemann, A.F.,Zychlinski, A.,Baldus, M.,Lange, A.,Griesinger, C.,Kolbe, M. (deposition date: 2010-03-09, release date: 2010-06-16, Last modification date: 2024-05-01) |
Primary citation | Poyraz, O.,Schmidt, H.,Seidel, K.,Delissen, F.,Ader, C.,Tenenboim, H.,Goosmann, C.,Laube, B.,Thunemann, 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., 17:788-792, 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 | SOLUTION NMR |
Structure validation
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