1cii

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1cii" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cii, resolution 3.0&Aring;" /> '''COLICIN IA'''<br /> ...)
Line 1: Line 1:
-
[[Image:1cii.gif|left|200px]]<br /><applet load="1cii" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1cii.gif|left|200px]]<br /><applet load="1cii" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1cii, resolution 3.0&Aring;" />
caption="1cii, resolution 3.0&Aring;" />
'''COLICIN IA'''<br />
'''COLICIN IA'''<br />
==Overview==
==Overview==
-
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.
+
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.
==About this Structure==
==About this Structure==
-
1CII is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CII OCA].
+
1CII is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CII OCA].
==Reference==
==Reference==
Line 22: Line 22:
[[Category: transmembrane protein]]
[[Category: transmembrane protein]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:29:19 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:28 2008''

Revision as of 10:06, 21 February 2008

Image:1cii.gif

1cii, resolution 3.0Å

Drag the structure with the mouse to rotate

COLICIN IA

Overview

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.

About this Structure

1CII is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of colicin Ia., Wiener M, Freymann D, Ghosh P, Stroud RM, Nature. 1997 Jan 30;385(6615):461-4. PMID:9009197

Page seeded by OCA on Thu Feb 21 12:06:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cii"
Personal tools