1oye: Difference between revisions

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New page: left|200px<br /><applet load="1oye" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oye, resolution 3.48Å" /> '''Structural Basis of ...
 
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[[Image:1oye.gif|left|200px]]<br /><applet load="1oye" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1oye.gif|left|200px]]<br /><applet load="1oye" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1oye, resolution 3.48&Aring;" />
caption="1oye, resolution 3.48&Aring;" />
'''Structural Basis of Multiple Binding Capacity of the AcrB multidrug Efflux Pump'''<br />
'''Structural Basis of Multiple Binding Capacity of the AcrB multidrug Efflux Pump'''<br />


==Overview==
==Overview==
Multidrug efflux pumps cause serious problems in cancer chemotherapy and, treatment of bacterial infections. Yet high-resolution structures of, ligand transporter complexes have previously been unavailable. We obtained, x-ray crystallographic structures of the trimeric AcrB pump from, Escherichia coli with four structurally diverse ligands. The structures, show that three molecules of ligands bind simultaneously to the extremely, large central cavity of 5000 cubic angstroms, primarily by hydrophobic, aromatic stacking and van der Waals interactions. Each ligand uses a, slightly different subset of AcrB residues for binding. The bound ligand, molecules often interact with each other, stabilizing the binding.
Multidrug efflux pumps cause serious problems in cancer chemotherapy and treatment of bacterial infections. Yet high-resolution structures of ligand transporter complexes have previously been unavailable. We obtained x-ray crystallographic structures of the trimeric AcrB pump from Escherichia coli with four structurally diverse ligands. The structures show that three molecules of ligands bind simultaneously to the extremely large central cavity of 5000 cubic angstroms, primarily by hydrophobic, aromatic stacking and van der Waals interactions. Each ligand uses a slightly different subset of AcrB residues for binding. The bound ligand molecules often interact with each other, stabilizing the binding.


==About this Structure==
==About this Structure==
1OYE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CPF as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OYE OCA].  
1OYE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CPF:'>CPF</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYE OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Jr., D.E.Koshland.]]
[[Category: Jr., D E.Koshland.]]
[[Category: McDermott, G.]]
[[Category: McDermott, G.]]
[[Category: Nikaido, H.]]
[[Category: Nikaido, H.]]
[[Category: Yu, E.W.]]
[[Category: Yu, E W.]]
[[Category: Zgurskaya, H.I.]]
[[Category: Zgurskaya, H I.]]
[[Category: CPF]]
[[Category: CPF]]
[[Category: membrane protein]]
[[Category: membrane protein]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:01 2008''

Revision as of 15:23, 21 February 2008

File:1oye.gif


1oye, resolution 3.48Å

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Structural Basis of Multiple Binding Capacity of the AcrB multidrug Efflux Pump

OverviewOverview

Multidrug efflux pumps cause serious problems in cancer chemotherapy and treatment of bacterial infections. Yet high-resolution structures of ligand transporter complexes have previously been unavailable. We obtained x-ray crystallographic structures of the trimeric AcrB pump from Escherichia coli with four structurally diverse ligands. The structures show that three molecules of ligands bind simultaneously to the extremely large central cavity of 5000 cubic angstroms, primarily by hydrophobic, aromatic stacking and van der Waals interactions. Each ligand uses a slightly different subset of AcrB residues for binding. The bound ligand molecules often interact with each other, stabilizing the binding.

About this StructureAbout this Structure

1OYE is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump., Yu EW, McDermott G, Zgurskaya HI, Nikaido H, Koshland DE Jr, Science. 2003 May 9;300(5621):976-80. PMID:12738864

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