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

This research was originally published in Journal of Biological Chemistry. Hiroyuki Akama, Misa Kanemaki, Masato Yoshimura, Tomitake Tsukihara, Tomoe Kashiwagi, Hiroshi Yoneyama, Shin-ichiro Narita, Atsushi Nakagawa and Taiji Nakae. Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa : Dual modes of membrane anchoring and occluded cavity end. Journal of Biological Chemistry. 2004; 279, 52816-52819. © the American Society for Biochemistry and Molecular Biology

Preliminary crystallographic analysis of the antibiotic discharge outer membrane lipoprotein OprM of Pseudomonas aeruginosa with an exceptionally long unit cell and complex lattice structure

The OprM subunit of the MexAB-OprM efflux pump in P. aeruginosa is an outer membrane-anchored lipoprotein. OprM crystals have been grown at 293 K in the presence of 2-methyl-2,4-propanediol and a combination of surfactants and diffracted to 2.56 Å resolution