2drd: Difference between revisions

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[[Image:2drd.gif|left|200px]]
[[Image:2drd.gif|left|200px]]


{{Structure
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|SITE=
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|LIGAND= <scene name='pdbligand=MIY:(4S,4AS,5AR,12AS)-4,7-BIS(DIMETHYLAMINO)-3,10,12,12A-TETRAHYDROXY-1,11-DIOXO-1,4,4A,5,5A,6,11,12A-OCTAHYDROTETRACENE-2-CARBOXAMIDE'>MIY</scene>
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|DOMAIN=
{{STRUCTURE_2drd| PDB=2drd  | SCENE= }}  
|RELATEDENTRY=[[2dhh|2DHH]], [[2dr6|2DR6]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2drd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2drd OCA], [http://www.ebi.ac.uk/pdbsum/2drd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2drd RCSB]</span>
}}


'''Crystal structure of a multidrug transporter reveal a functionally rotating mechanism'''
'''Crystal structure of a multidrug transporter reveal a functionally rotating mechanism'''
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[[Category: Nakashima, R.]]
[[Category: Nakashima, R.]]
[[Category: Yamashita, E.]]
[[Category: Yamashita, E.]]
[[Category: antiporter]]
[[Category: Antiporter]]
[[Category: drug resistance]]
[[Category: Drug resistance]]
[[Category: exporter]]
[[Category: Exporter]]
[[Category: membrane protein]]
[[Category: Membrane protein]]
[[Category: membrane transporter]]
[[Category: Membrane transporter]]
[[Category: multidrug efflux]]
[[Category: Multidrug efflux]]
[[Category: transporter]]
[[Category: Transporter]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:38:24 2008''

Revision as of 01:00, 4 May 2008

File:2drd.gif

Template:STRUCTURE 2drd

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. 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 Page seeded by OCA on Sun May 4 01:00:17 2008

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