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Full-Text Articles in Medicinal-Pharmaceutical Chemistry

Functional Cloning And Characterization Of The Multidrug Efflux Pumps Norm From Neisseria Gonorrhoeae And Ydhe From Escherichia Coli, Feng Long, Corrinne Rouquette-Loughlin, William M. Shafer, Edward Yu Jan 2008

Functional Cloning And Characterization Of The Multidrug Efflux Pumps Norm From Neisseria Gonorrhoeae And Ydhe From Escherichia Coli, Feng Long, Corrinne Rouquette-Loughlin, William M. Shafer, Edward Yu

Physics and Astronomy Publications

Active efflux of antimicrobial agents is one of the most important adapted strategies that bacteria use to defend against antimicrobial factors that are present in their environment. The NorM protein of Neisseria gonorrhoeae and the YdhE protein of Escherichia coli have been proposed to be multidrug efflux pumps that belong to the multidrug and toxic compound extrusion (MATE) family. In order to determine their antimicrobial export capabilities, we cloned, expressed, and purified these two efflux proteins and characterized their functions both in vivo and in vitro. E. coli strains expressing norM or ydhE showed elevated (twofold or greater) resistance to ...


Conformational Change Of The Acrr Regulator Reveals A Possible Mechanism Of Induction, Ruoyu Gu, Ming Li, Chih-Chia Su, Feng Long, Matthew D. Routh, Feng Yang, Gerry Mcdermott, Edward Yu Jan 2008

Conformational Change Of The Acrr Regulator Reveals A Possible Mechanism Of Induction, Ruoyu Gu, Ming Li, Chih-Chia Su, Feng Long, Matthew D. Routh, Feng Yang, Gerry Mcdermott, Edward Yu

Physics and Astronomy Publications

The Escherichia coli AcrR multidrug-binding protein represses transcription of acrAB and is induced by many structurally unrelated cytotoxic compounds. The crystal structure of AcrR in space group P2221 has been reported previously. This P2221 structure has provided direct information about the multidrug-binding site and important residues for drug recognition. Here, a crystal structure of this regulator in space group P31 is presented. Comparison of the two AcrR structures reveals possible mechanisms of ligand binding and AcrR regulation.


Crystallization And Preliminary X-Ray Diffraction Analysis Of The Multidrug Efflux Transporter Norm From Neisseria Gonorrhoeae, Chih-Chia Su, Feng Long, Gerry Mcdermott, William M. Shafer, Edward Yu Jan 2008

Crystallization And Preliminary X-Ray Diffraction Analysis Of The Multidrug Efflux Transporter Norm From Neisseria Gonorrhoeae, Chih-Chia Su, Feng Long, Gerry Mcdermott, William M. Shafer, Edward Yu

Physics and Astronomy Publications

The crystallization and preliminary X-ray data analysis of the NorM multidrug efflux pump produced by Neisseria gonorrhoeae are reported. NorM is a cytoplasmic membrane protein that consists of 459 amino-acid residues. It is a member of the recently classified multidrug and toxic compound extrusion (MATE) family of transporters and recognizes a number of cationic toxic compounds such as ethidium bromide, acriflavin, 2-N-methylellipticinium and ciprofloxacin. Recombinant NorM protein was expressed in Escherichia coli and purified by metal-affinity and gel-filtration chromatography. The protein was crystallized using hanging-drop vapor diffusion. X-ray diffraction data were collected from cryocooled crystals at a synchrotron ...