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2X9C

Crystal structure of a soluble PrgI mutant from Salmonella Typhimurium

Summary for 2X9C
Entry DOI10.2210/pdb2x9c/pdb
Related2KV7
DescriptorPROTEIN PRGI (2 entities in total)
Functional Keywordsneedle protomer, protein transport, bacterial pathogenesis
Biological sourceSALMONELLA TYPHIMURIUM
Total number of polymer chains2
Total formula weight18182.07
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 citationPoyraz, 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: 20543831
DOI: 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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