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Keywords
(8)
cryo-electron microscopy
Gram Negative Bacteria
Homology Modeling
pseudomonas syringae
Type Iii Secretion
C Terminal Domain
Face To Face
Inner Membrane
Related Publications
(3)
New structural insights into the bacterial type III secretion system
Structural analysis of a prototypical ATPase from the type III secretion system
Characterization of the Yersinia enterocolitica Type III Secretion ATPase YscN and Its Regulator, YscL
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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
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Double hexameric ring assembly of the type III protein translocase ATPase HrcN
(
Citations: 16
)
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Shirley A. Muller
,
Charalambos Pozidis
,
Remington Stone
,
Christian Meesters
,
Mohamed Chami
,
Andreas Engel
,
Anastassios Economou
,
Henning Stahlberg
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
DOI:
10.1111/j.1365-2958.2006.05219.x
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)
Citation Context
(6)
... In the plant-like T3SSs, the homologous HrcN ATPase forms a double hexameric head-to-head assembly located in the center of the entrance to the translocation pore
...
Wieslaw Swietnicki
,
et al.
Identification of Small-Molecule Inhibitors of Yersinia pestis Type II...
...stacks, as was found for other dodecameric traffic ATPases (
Müller et al., 2006
)...
Daniela Buttner
,
et al.
Type III Protein Secretion in Plant Pathogenic Bacteria
...The ATPase forms a ring structure associated with the secretion apparatus at the inner bacterial membrane and was predicted to provide the energy for the secretion process (
50
, 74, 75)...
Christian Lorenz
,
et al.
Functional Characterization of the Type III Secretion ATPase HrcN from...
...T3S ATPases oligomerize as a dodecamer at the inner membrane, and this oligomeric state has been associated with enhanced enzymatic activity (
30
, 33)...
...The high-molecular-weight bands could be consistent with the formation of dodecamers, which have been described for other T3S ATPases (
30
, 33)...
...CdsN hydrolyzes ATP in a linear, time-dependent manner at a rate of 0.55 0.06 mol phosphate min1 mg1, which is typical of rates for other T3S ATPases (3, 5). At higher protein concentrations, ATPase activity decreased, suggesting a positive cooperativity of CdsN, which was previously described for other T3S ATPases (3, 5,
30
)...
...The presence of high-molecular-weight forms of CdsN may correspond to dodecamers that were reported previously for other T3S ATPases (
30
)...
Chris B. Stone
,
et al.
Characterization of the Putative Type III Secretion ATPase CdsN (Cpn07...
...8 n
...
Guy R. Cornelis
.
The type III secretion injectisome
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Citations
(16)
Identification of Small-Molecule Inhibitors of Yersinia pestis Type III Secretion System YscN ATPase
Wieslaw Swietnicki
,
Daniel Carmany
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Michael Retford
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