2drd: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:2drd.gif|left|200px]] | [[Image:2drd.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_2drd", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_2drd| PDB=2drd | SCENE= }} | |||
}} | |||
'''Crystal structure of a multidrug transporter reveal a functionally rotating mechanism''' | '''Crystal structure of a multidrug transporter reveal a functionally rotating mechanism''' | ||
Line 29: | Line 26: | ||
[[Category: Nakashima, R.]] | [[Category: Nakashima, R.]] | ||
[[Category: Yamashita, E.]] | [[Category: Yamashita, E.]] | ||
[[Category: | [[Category: Antiporter]] | ||
[[Category: | [[Category: Drug resistance]] | ||
[[Category: | [[Category: Exporter]] | ||
[[Category: | [[Category: Membrane protein]] | ||
[[Category: | [[Category: Membrane transporter]] | ||
[[Category: | [[Category: Multidrug efflux]] | ||
[[Category: | [[Category: Transporter]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:00:17 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 01:00, 4 May 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. 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