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

@article{Akama2004CrystalSO,
  title={Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded cavity end.},
  author={Hiroyuki Akama and Misa Kanemaki and Masato Yoshimura and Tomitake Tsukihara and Tomoe Kashiwagi and Hiroshi Yoneyama and Shin-ichiro Narita and Atsushi Nakagawa and Taiji Nakae},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 51},
  pages={52816-9}
}
The OprM lipoprotein of Pseudomonas aeruginosa is a member of the MexAB-OprM xenobiotic-antibiotic transporter subunits that is assumed to serve as the drug discharge duct across the outer membrane. The channel structure must differ from that of the porin-type open pore because the protein facilitates the exit of antibiotics but not the entry. For better understanding of the structure-function linkage of this important pump subunit, we studied the x-ray crystallographic structure of OprM at the… CONTINUE READING
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