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Medicinal-Pharmaceutical Chemistry Commons

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Physics and Astronomy Publications

Biochemistry, Biophysics, and Structural Biology

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Full-Text Articles in Medicinal-Pharmaceutical Chemistry

Crystal Structure Of The Neisseria Gonorrhoeae Mtrd Inner Membrane Multidrug Efflux Pump, Jani Reddy Bolla, Chih-Chia Su, Sylvia V. Do, Pattathil Radhakrishnan, Nitin Kumar, Feng Long, Tsung-Han Chou, Jared A. Delmar, Hsiang-Ting Lei, Kanagalaghatta R. Rajashankar, William M. Shafer, Edward Yu Jan 2014

Crystal Structure Of The Neisseria Gonorrhoeae Mtrd Inner Membrane Multidrug Efflux Pump, Jani Reddy Bolla, Chih-Chia Su, Sylvia V. Do, Pattathil Radhakrishnan, Nitin Kumar, Feng Long, Tsung-Han Chou, Jared A. Delmar, Hsiang-Ting Lei, Kanagalaghatta R. Rajashankar, William M. Shafer, Edward Yu

Physics and Astronomy Publications

Neisseria gonorrhoeae is an obligate human pathogen and the causative agent of the sexually-transmitted disease gonorrhea. The control of this disease has been compromised by the increasing proportion of infections due to antibiotic-resistant strains, which are growing at an alarming rate. The MtrCDE tripartite multidrug efflux pump, belonging to the hydrophobic and amphiphilic efflux resistance-nodulation-cell division (HAE-RND) family, spans both the inner and outer membranes of N. gonorrhoeae and confers resistance to a variety of antibiotics and toxic compounds. We here report the crystal structure of the inner membrane MtrD multidrug efflux pump, which reveals a novel structural feature that ...


Crystal Structure Of The Open State Of The Neisseria Gonorrhoeae Mtre Outer Membrane Channel, Hsiang-Ting Lei, Tsung-Han Chou, Chih-Chia Su, Jani Reddy Bolla, Nitin Kumar, Pattathil Radhakrishnan, Feng Long, Jared A. Delmar, Sylvia V. Do, Kanagalaghatta R. Rajashankar, William M. Shafer, Edward Yu Jan 2014

Crystal Structure Of The Open State Of The Neisseria Gonorrhoeae Mtre Outer Membrane Channel, Hsiang-Ting Lei, Tsung-Han Chou, Chih-Chia Su, Jani Reddy Bolla, Nitin Kumar, Pattathil Radhakrishnan, Feng Long, Jared A. Delmar, Sylvia V. Do, Kanagalaghatta R. Rajashankar, William M. Shafer, Edward Yu

Physics and Astronomy Publications

Active efflux of antimicrobial agents is one of the most important strategies used by bacteria to defend against antimicrobial factors present in their environment. Mediating many cases of antibiotic resistance are transmembrane efflux pumps, composed of one or more proteins. The Neisseria gonorrhoeae MtrCDE tripartite multidrug efflux pump, belonging to the hydrophobic and amphiphilic efflux resistance-nodulation-cell division (HAE-RND) family, spans both the inner and outer membranes of N. gonorrhoeae and confers resistance to a variety of antibiotics and toxic compounds. We here describe the crystal structure of N. gonorrhoeae MtrE, the outer membrane component of the MtrCDE tripartite multidrug efflux ...


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 ...