2drd: Difference between revisions

Revision as of 18:01, 21 February 2008

Crystal structure of a multidrug transporter reveal a functionally rotating mechanism

OverviewOverview

AcrB is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA. Here we describe crystal structures of AcrB with and without substrates. The AcrB-drug complex consists of three protomers, each of which has a different conformation corresponding to one of the three functional states of the transport cycle. Bound substrate was found in the periplasmic domain of one of the three protomers. The voluminous binding pocket is aromatic and allows multi-site binding. The structures indicate that drugs are exported by a three-step functionally rotating mechanism in which substrates undergo ordered binding change.

About this StructureAbout this Structure

2DRD is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of a multidrug transporter reveal a functionally rotating mechanism., Murakami S, Nakashima R, Yamashita E, Matsumoto T, Yamaguchi A, Nature. 2006 Sep 14;443(7108):173-9. Epub 2006 Aug 16. PMID:16915237

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 ==Overview==
-AcrB is a principal multidrug efflux transporter in Escherichia coli that, cooperates with an outer-membrane channel, TolC, and a membrane-fusion, protein, AcrA. Here we describe crystal structures of AcrB with and, without substrates. The AcrB-drug complex consists of three protomers, each of which has a different conformation corresponding to one of the, three functional states of the transport cycle. Bound substrate was found, in the periplasmic domain of one of the three protomers. The voluminous, binding pocket is aromatic and allows multi-site binding. The structures, indicate that drugs are exported by a three-step functionally rotating, mechanism in which substrates undergo ordered binding change.
+AcrB is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA. Here we describe crystal structures of AcrB with and without substrates. The AcrB-drug complex consists of three protomers, each of which has a different conformation corresponding to one of the three functional states of the transport cycle. Bound substrate was found in the periplasmic domain of one of the three protomers. The voluminous binding pocket is aromatic and allows multi-site binding. The structures indicate that drugs are exported by a three-step functionally rotating mechanism in which substrates undergo ordered binding change.
 ==About this Structure==
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 [[Category: transporter]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:22:08 2008''
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