2dr6

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{{STRUCTURE_2dr6| PDB=2dr6 | SCENE= }}
{{STRUCTURE_2dr6| PDB=2dr6 | SCENE= }}
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'''Crystal structure of a multidrug transporter reveal a functionally rotating mechanism'''
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===Crystal structure of a multidrug transporter reveal a functionally rotating mechanism===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_16915237}}
==About this Structure==
==About this Structure==
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[[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 Jul 28 06:38:15 2008''

Revision as of 03:38, 28 July 2008

Image:2dr6.png

Template:STRUCTURE 2dr6

Crystal structure of a multidrug transporter reveal a functionally rotating mechanism

Template:ABSTRACT PUBMED 16915237

About this Structure

2DR6 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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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