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Double hexameric ring assembly of the type III protein translocase ATPase HrcN

Double hexameric ring assembly of the type III protein translocase ATPase HrcN,10.1111/j.1365-2958.2006.05219.x,Molecular Microbiology,Shirley A. Mull

Double hexameric ring assembly of the type III protein translocase ATPase HrcN   (Citations: 16)
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Summary The specialized type III secretion (T3S) apparatus of pathogenic and symbiotic Gram-negative bacteria comprises a complex transmembrane organelle and an ATPase homologous to the F1-ATPase b 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 (HrcN12) deter- mined to 1.6 nm by cryo-electron microscopy is presented. HrcN12 comprises two hexameric rings that are probably stacked face-to-face by the associa- tion 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 F1-b- ATPase. A model for its incorporation within the T3S apparatus is presented.
Journal: Molecular Microbiology - MOL MICROBIOL , vol. 61, no. 1, pp. 119-125, 2006
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