Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli (Q27667059)

2

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Michael T Zimmermann

3

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Kanagalaghatta R Rajashankar

4

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Robert L Jernigan

5

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Edward W Yu

Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport

6

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language of work or name

English

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publication date

24 February 2011

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published in

Nature

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volume

470

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issue

7335

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page(s)

558-62

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cites work

1 reference

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Crystal Structure of the Membrane Fusion Protein CusB from Escherichia coli

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Crystal structure of the multidrug exporter MexB from Pseudomonas aeruginosa

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The assembled structure of a complete tripartite bacterial multidrug efflux pump

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Unusual Cu(I)/Ag(I) coordination ofEscherichia coliCusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy

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Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors

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Structural Basis of Multiple Drug-Binding Capacity of the AcrB Multidrug Efflux Pump

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Crystal structure of bacterial multidrug efflux transporter AcrB

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Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export

20 March 2017

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Structure of the periplasmic component of a bacterial drug efflux pump

20 March 2017

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Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone.

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Conformation of the AcrB multidrug efflux pump in mutants of the putative proton relay pathway

29 September 2017

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Conformational flexibility in the multidrug efflux system protein AcrA.

29 September 2017

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A periplasmic drug-binding site of the AcrB multidrug efflux pump: a crystallographic and site-directed mutagenesis study.

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Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded cavity end.

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Crystal structure of the membrane fusion protein, MexA, of the multidrug transporter in Pseudomonas aeruginosa.

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Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli

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Crystal structures of a multidrug transporter reveal a functionally rotating mechanism.

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Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism.

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Genetic evidence for functional interactions between TolC and AcrA proteins of a major antibiotic efflux pump of Escherichia coli.

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The product of the ybdE gene of the Escherichia coli chromosome is involved in detoxification of silver ions

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PubMed

https://pubmed.ncbi.nlm.nih.gov/21350490