Gating properties of channels formed by colicin Ia in planar lipid bilayer membranes

1988 ◽  
Vol 105 (2) ◽  
pp. 143-153 ◽  
Author(s):  
Romildo A. Nogueira ◽  
A. Varanda
1983 ◽  
Vol 7 (4) ◽  
pp. 299-310 ◽  
Author(s):  
Pierre Tancrède ◽  
Paul Paquin ◽  
André Houle ◽  
Roger M. Leblanc

2009 ◽  
Vol 106 (51) ◽  
pp. 21990-21995 ◽  
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E. Udho ◽  
K. S. Jakes ◽  
S. K. Buchanan ◽  
K. J. James ◽  
X. Jiang ◽  
...  

Nature ◽  
1983 ◽  
Vol 303 (5913) ◽  
pp. 172-175 ◽  
Author(s):  
Bruce K. Krueger ◽  
Jennings F. Worley ◽  
Robert J. French

1982 ◽  
Vol 688 (3) ◽  
pp. 808-810 ◽  
Author(s):  
Joaquim Procopio ◽  
Wamberto A. Varanda ◽  
JoséA. Fornes

2006 ◽  
Vol 150 (2) ◽  
pp. 249-254 ◽  
Author(s):  
Hajime Ikigai ◽  
Toshihisa Ono ◽  
Masashi Iwata ◽  
Taiji Nakae ◽  
Tadakatsu Shimamura

2009 ◽  
Vol 284 (24) ◽  
pp. 16126-16134 ◽  
Author(s):  
Sarah L. Greig ◽  
Mazdak Radjainia ◽  
Alok K. Mitra

Colicin Ia is a soluble, harpoon-shaped bacteriocin which translocates across the periplasmic space of sensitive Escherichia coli cell by parasitizing an outer membrane receptor and forms voltage-gated ion channels in the inner membrane. This process leads to cell death, which has been thought to be caused by a single colicin Ia molecule. To directly visualize the three-dimensional structure of the channel, we generated two-dimensional crystals of colicin Ia inserted in lipid-bilayer membranes and determined a ∼17 three-dimensional model by electron crystallography. Supported by velocity sedimentation, chemical cross-linking and single-particle image analysis, the three-dimensional structure is a crown-shaped oligomer enclosing a ∼35 Å-wide extrabilayer vestibule. Our study suggests that lipid insertion instigates a global conformational change in colicin Ia and that more than one molecule participates in the channel architecture with the vestibule, possibly facilitating the known large scale peptide translocation upon channel opening.


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