Mueller, Shirley A.Pozidis, CharalambosStone, RemingtonMeesters, ChristianChami, MohamedEngel, AndreasEconomou, AnastassiosStahlberg, Henning2020-02-132020-02-132020-02-132006-06-0110.1111/j.1365-2958.2006.05219.xhttps://infoscience.epfl.ch/handle/20.500.14299/165377The specialized type III secretion (T3S) apparatus of pathogenic and symbiotic Gram-negative bacteria comprises a complex transmembrane organelle and an ATPase homologous to the F-1-ATPase beta subunit. The T3S ATPase HrcN of Pseudomonas syringae associates with the inner membrane, and its ATP hydrolytic activity is stimulated by dodecamerization. The structure of dodecameric HrcN (HrcN(12)) determined to 1.6 nm by cryo-electron microscopy is presented. HrcN(12) comprises two hexameric rings that are probably stacked face-to-face by the association of their C-terminal domains. It is 11.5 +/- 1.0 nm in diameter, 12.0 +/- 2.0 nm high and has a 2.0-3.8 nm wide inner channel. This structure is compared to a homology model based on the structure of the F-1-beta-ATPase. A model for its incorporation within the T3S apparatus is presented.Double hexameric ring assembly of the type III protein translocase ATPase HrcNtext::journal::journal article::research article