 |
PDBsum entry 1cii
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transmembrane protein
|
PDB id
|
|
|
|
1cii
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of colicin ia.
|
|
|
Authors
|
|
M.Wiener,
D.Freymann,
P.Ghosh,
R.M.Stroud.
|
|
|
Ref.
|
|
Nature, 1997,
385,
461-464.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The ion-channel forming colicins A, B, E1, Ia, Ib and N all kill bacterial cells
selectively by co-opting bacterial active-transport pathways and forming
voltage-gated ion conducting channels across the plasma membrane of the target
bacterium. The crystal structure of colicin Ia reveals a molecule 210 A long
with three distinct functional domains arranged along a backbone of two
extraordinarily long alpha-helices. A central domain at the bend of the
hairpin-like structure mediates specific recognition and binding to an
outer-membrane receptor. A second domain mediates translocation across the outer
membrane via the TonB transport pathway; the TonB-box recognition element of
colicin Ia is on one side of three 80 A-long helices arranged as a helical
sheet. A third domain is made up of 10 alpha-helices which form a
voltage-activated and voltage-gated ion conducting channel across the plasma
membrane of the target cell. The two 160 A-long alpha-helices that link the
receptor-binding domain to the other domains enable the colicin Ia molecule to
span the periplasmic space and contact both the outer and plasma membranes
simultaneously during function.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
The domain structure of the ion channel-Forming protein colicin ia.
|
|
|
Authors
|
|
P.Ghosh,
S.F.Mel,
R.M.Stroud.
|
|
|
Ref.
|
|
Nat Struct Biol, 1994,
1,
597-604.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #2
|
|
|
Title
|
|
|
|
|
Author
|
|
P.Ghosh.
|
|
|
Ref.
|
|
the structure and function ...
|
|
|
|
|
|
|
|
