例如:"lncRNA", "apoptosis", "WRKY"

Crystal structure of AcrB in complex with a single transmembrane subunit reveals another twist.

Structure. 2007 Dec;15(12):1663-73
Susanna Törnroth-Horsefield 1 , Pontus Gourdon , Rob Horsefield , Lars Brive , Natsuko Yamamoto , Hirotada Mori , Arjan Snijder , Richard Neutze
Susanna Törnroth-Horsefield 1 , Pontus Gourdon , Rob Horsefield , Lars Brive , Natsuko Yamamoto , Hirotada Mori , Arjan Snijder , Richard Neutze
+ et al

[No authors listed]

Author information
  • 1 Department of Chemistry, Biochemistry and Biophysics, Gothenburg University, 40530 Gothenburg, Sweden. susanna.tornroth@chem.gu.se

摘要


Bacterial drug resistance is a serious concern for human health. Multidrug efflux pumps export a broad variety of substrates out of the cell and thereby convey resistance to the host. In Escherichia coli, the AcrB:AcrA:TolC efflux complex forms a principal transporter for which structures of the individual component proteins have been determined in isolation. Here, we present the X-ray structure of AcrB in complex with a single transmembrane protein, assigned by mass spectrometry as YajC. A specific rotation of the periplasmic porter domain of AcrB is also revealed, consistent with the hypothesized "twist-to-open" mechanism for TolC activation. Growth experiments with yajc-deleted E. coli reveal a modest increase in the organism's susceptibility to beta-lactam antibiotics, but this effect could not conclusively be attributed to the loss of interactions between YajC and AcrB.