4dx5

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[[Image:4dx5.jpg|left|200px]]
 
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{{STRUCTURE_4dx5| PDB=4dx5 | SCENE= }}
{{STRUCTURE_4dx5| PDB=4dx5 | SCENE= }}
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===Transport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loop===
===Transport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loop===
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{{ABSTRACT_PUBMED_22451937}}
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==Function==
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[[http://www.uniprot.org/uniprot/ACRB_ECOLI ACRB_ECOLI]] AcrAB is a drug efflux protein with a broad substrate specificity.<ref>PMID:16915237</ref> <ref>PMID:16946072</ref> <ref>PMID:17194213</ref>
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{{ABSTRACT_PUBMED_22451937}}
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==About this Structure==
==About this Structure==
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[[4dx5]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DX5 OCA].
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[[4dx5]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DX5 OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:022451937</ref><references group="xtra"/>
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<ref group="xtra">PMID:022451937</ref><references group="xtra"/><references/>
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[[Category: Escherichia coli]]
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[[Category: Ecoli]]
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[[Category: Synthetic construct]]
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[[Category: Bohnert, J A.]]
[[Category: Bohnert, J A.]]
[[Category: Brandstaetter, L.]]
[[Category: Brandstaetter, L.]]

Revision as of 06:26, 29 January 2014

Template:STRUCTURE 4dx5

Contents

Transport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loop

Template:ABSTRACT PUBMED 22451937

Function

[ACRB_ECOLI] AcrAB is a drug efflux protein with a broad substrate specificity.[1] [2] [3]

About this Structure

4dx5 is a 5 chain structure with sequence from [1] and Ecoli. Full crystallographic information is available from OCA.

Reference

  • Eicher T, Cha HJ, Seeger MA, Brandstatter L, El-Delik J, Bohnert JA, Kern WV, Verrey F, Grutter MG, Diederichs K, Pos KM. Transport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loop. Proc Natl Acad Sci U S A. 2012 Apr 10;109(15):5687-92. Epub 2012 Mar 26. PMID:22451937 doi:10.1073/pnas.1114944109
  1. ↑ Murakami S, Nakashima R, Yamashita E, Matsumoto T, Yamaguchi A. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature. 2006 Sep 14;443(7108):173-9. Epub 2006 Aug 16. PMID:16915237 doi:10.1038/nature05076
  2. ↑ Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, Pos KM. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science. 2006 Sep 1;313(5791):1295-8. PMID:16946072 doi:313/5791/1295
  3. ↑ Sennhauser G, Amstutz P, Briand C, Storchenegger O, Grutter MG. Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors. PLoS Biol. 2007 Jan;5(1):e7. PMID:17194213 doi:10.1371/journal.pbio.0050007

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