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TitleDouble hexameric ring assembly of the type III protein translocase ATPase HrcN.
Journal, issue, pagesMol Microbiol, Vol. 61, Issue 1, Page 119-125, Year 2006
Publish dateSep 29, 2006
AuthorsShirley A Müller / Charalambos Pozidis / Remington Stone / Christian Meesters / Mohamed Chami / Andreas Engel / Anastassios Economou / Henning Stahlberg /
PubMed AbstractThe 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 beta ...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 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 (HrcN12) determined to 1.6 nm by cryo-electron microscopy is presented. HrcN12 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 F1-beta-ATPase. A model for its incorporation within the T3S apparatus is presented.
External linksMol Microbiol / PubMed:16824099
MethodsEM (single particle)
Resolution16.0 Å
Structure data

EMDB-1160:
Double hexameric ring assembly of the type III protein translocase ATPase HrcN.
Method: EM (single particle) / Resolution: 16.0 Å

Source
  • Pseudomonas syringae pv. phaseolicola (bacteria)

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