2hrt
From Proteopedia
(New page: 200px<br /><applet load="2hrt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hrt, resolution 3.00Å" /> '''Asymmetric structure...) |
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| - | [[Image:2hrt.jpg|left|200px]]<br /><applet load="2hrt" size=" | + | [[Image:2hrt.jpg|left|200px]]<br /><applet load="2hrt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2hrt, resolution 3.00Å" /> | caption="2hrt, resolution 3.00Å" /> | ||
'''Asymmetric structure of trimeric AcrB from Escherichia coli'''<br /> | '''Asymmetric structure of trimeric AcrB from Escherichia coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The AcrA/AcrB/TolC complex spans the inner and outer membranes of | + | The AcrA/AcrB/TolC complex spans the inner and outer membranes of Escherichia coli and serves as its major drug-resistance pump. Driven by the proton motive force, it mediates the efflux of bile salts, detergents, organic solvents, and many structurally unrelated antibiotics. Here, we report a crystallographic structure of trimeric AcrB determined at 2.9 and 3.0 angstrom resolution in space groups that allow asymmetry of the monomers. This structure reveals three different monomer conformations representing consecutive states in a transport cycle. The structural data imply an alternating access mechanism and a novel peristaltic mode of drug transport by this type of transporter. |
==About this Structure== | ==About this Structure== | ||
| - | 2HRT 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 FLC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2HRT 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=FLC:'>FLC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HRT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Diederichs, K.]] | [[Category: Diederichs, K.]] | ||
[[Category: Eicher, T.]] | [[Category: Eicher, T.]] | ||
| - | [[Category: Pos, K | + | [[Category: Pos, K M.]] |
[[Category: Schiefner, A.]] | [[Category: Schiefner, A.]] | ||
| - | [[Category: Seeger, M | + | [[Category: Seeger, M A.]] |
[[Category: Verrey, F.]] | [[Category: Verrey, F.]] | ||
[[Category: FLC]] | [[Category: FLC]] | ||
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[[Category: tolc]] | [[Category: tolc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:45:04 2008'' |
Revision as of 15:45, 21 February 2008
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Asymmetric structure of trimeric AcrB from Escherichia coli
Overview
The AcrA/AcrB/TolC complex spans the inner and outer membranes of Escherichia coli and serves as its major drug-resistance pump. Driven by the proton motive force, it mediates the efflux of bile salts, detergents, organic solvents, and many structurally unrelated antibiotics. Here, we report a crystallographic structure of trimeric AcrB determined at 2.9 and 3.0 angstrom resolution in space groups that allow asymmetry of the monomers. This structure reveals three different monomer conformations representing consecutive states in a transport cycle. The structural data imply an alternating access mechanism and a novel peristaltic mode of drug transport by this type of transporter.
About this Structure
2HRT is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism., Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, Pos KM, Science. 2006 Sep 1;313(5791):1295-8. PMID:16946072
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