2X9C

Crystal structure of a soluble PrgI mutant from Salmonella Typhimurium

2X9C の概要

• エントリーDOI: 10.2210/pdb2x9c/pdb
• 関連するPDBエントリー: 2KV7
• 分子名称: PROTEIN PRGI (2 entities in total)
• 機能のキーワード: needle protomer, protein transport, bacterial pathogenesis
• 由来する生物種: SALMONELLA TYPHIMURIUM
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18182.07

構造登録者

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. (登録日: 2010-03-15, 公開日: 2010-06-16, 最終更新日: 2023-12-20)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2.45 Å)