Crystal structure of the membrane-fusion protein of the multidrug efflux pump

Takanori Matsuura1, Hiroaki Akama2, Tomitake Tsukihara1, Atsushi Nakagawa1, Taiji Nakae2

1Institute for Protein Research, Osaka University,
2Department of Molecular Life Science, Tokai University School of Medicine

Gordon Research Conference on Bacterial Cell Surfaces (New London, NH, USA, 2004.6.27-7.2)

The MexA protein is an essential component of the MexAB-OprM efflux pump that confers multidrug resistance to the Pseudomonas aeruginosa cells. We studied the crystal structure of MexA at 2.4 Å resolution. The gross crystal structure of MexA exhibited unforeseen assembly of 13 protomers in which 6-mer and 7-mer were joined together at one end by a pseudo two-fold image. The protomer had tandem arrangement of three domains plus poorly solved one more domain: α-helical coiled-coil domain, globular β-domain, α+β-domain and disorder domain, respectively. Based on the result, we discuss the model of the MexAB-OprM pump assembly.

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MATSUURA Takanori (Please change the mark “%” to “@”)

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