1yc9: Difference between revisions

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[[Image:1yc9.~~gif~~|left|200px]]

[[Image:1yc9.png|left|200px]]

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~~'''~~The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 resolution~~'''~~

===The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 resolution===

~~==Overview==~~

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~~Multidrug resistance in Gram-negative bacteria arises in part from the activities of tripartite drug efflux pumps. In the pathogen Vibrio cholerae~~, ~~one such pump comprises the inner membrane proton antiporter VceB~~, the ~~periplasmic adaptor VceA, and~~ the ~~outer membrane channel VceC. Here, we report the crystal structure of VceC~~ at 1.~~8 A resolution~~. ~~The trimeric VceC~~ is ~~organized in~~ the ~~crystal lattice within laminar arrays that resemble membranes~~. ~~A well resolved detergent molecule within this array interacts with the transmembrane beta~~-~~barrel domain in a fashion that may mimic protein~~-lipopolysaccharide contacts. Our analyses of the external surfaces of VceC and other channel proteins suggest that different classes of efflux pumps have distinct architectures. We discuss the implications of these findings for mechanisms of drug and protein export.

The line below this paragraph, {{ABSTRACT_PUBMED_15684414}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15684414 is the PubMed ID number.

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==About this Structure==

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[[Category: Outer membrane protein]]

[[Category: Vibrio cholerae]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 16~~:08:37 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:20:45 2008''

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-[[Image:1yc9.gif|left|200px]]
+{{Seed}}
+[[Image:1yc9.png|left|200px]]
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 {{STRUCTURE_1yc9|  PDB=1yc9  |  SCENE=  }}
-'''The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 resolution'''
+===The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 resolution===
-==Overview==
+<!--
-Multidrug resistance in Gram-negative bacteria arises in part from the activities of tripartite drug efflux pumps. In the pathogen Vibrio cholerae, one such pump comprises the inner membrane proton antiporter VceB, the periplasmic adaptor VceA, and the outer membrane channel VceC. Here, we report the crystal structure of VceC at 1.8 A resolution. The trimeric VceC is organized in the crystal lattice within laminar arrays that resemble membranes. A well resolved detergent molecule within this array interacts with the transmembrane beta-barrel domain in a fashion that may mimic protein-lipopolysaccharide contacts. Our analyses of the external surfaces of VceC and other channel proteins suggest that different classes of efflux pumps have distinct architectures. We discuss the implications of these findings for mechanisms of drug and protein export.
+The line below this paragraph, {{ABSTRACT_PUBMED_15684414}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15684414 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15684414}}
 ==About this Structure==
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 [[Category: Outer membrane protein]]
 [[Category: Vibrio cholerae]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:08:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:20:45 2008''