1yc9
From Proteopedia
(New page: 200px<br /><applet load="1yc9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yc9, resolution 1.80Å" /> '''The crystal structur...) |
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| - | [[Image:1yc9.gif|left|200px]]<br /><applet load="1yc9" size=" | + | [[Image:1yc9.gif|left|200px]]<br /><applet load="1yc9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yc9, resolution 1.80Å" /> | caption="1yc9, resolution 1.80Å" /> | ||
'''The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 resolution'''<br /> | '''The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Multidrug resistance in Gram-negative bacteria arises in part from the | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1YC9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae] with BOG and HG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1YC9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae] with <scene name='pdbligand=BOG:'>BOG</scene> and <scene name='pdbligand=HG:'>HG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YC9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vibrio cholerae]] | [[Category: Vibrio cholerae]] | ||
| - | [[Category: Borges-Walmsley, M | + | [[Category: Borges-Walmsley, M I.]] |
[[Category: Du, D.]] | [[Category: Du, D.]] | ||
[[Category: Federici, L.]] | [[Category: Federici, L.]] | ||
[[Category: Fernandez-Recio, J.]] | [[Category: Fernandez-Recio, J.]] | ||
| - | [[Category: Luisi, B | + | [[Category: Luisi, B F.]] |
[[Category: Matsumura, H.]] | [[Category: Matsumura, H.]] | ||
| - | [[Category: McKeegan, K | + | [[Category: McKeegan, K S.]] |
[[Category: Walas, F.]] | [[Category: Walas, F.]] | ||
| - | [[Category: Walmsley, A | + | [[Category: Walmsley, A R.]] |
[[Category: BOG]] | [[Category: BOG]] | ||
[[Category: HG]] | [[Category: HG]] | ||
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[[Category: vibrio cholerae]] | [[Category: vibrio cholerae]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:50 2008'' |
Revision as of 14:03, 21 February 2008
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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.
About this Structure
1YC9 is a Single protein structure of sequence from Vibrio cholerae with and as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 A resolution., Federici L, Du D, Walas F, Matsumura H, Fernandez-Recio J, McKeegan KS, Borges-Walmsley MI, Luisi BF, Walmsley AR, J Biol Chem. 2005 Apr 15;280(15):15307-14. Epub 2005 Jan 31. PMID:15684414
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