2RDD

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

(2007) Structure 15: 1663-1673

• PubMed: 18073115 Search on PubMed
• DOI: https://doi.org/10.1016/j.str.2007.09.023
• Primary Citation of Related Structures:  
  2RDD


• PubMed Abstract: 
  

  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.

   View More

---

Organizational Affiliation: 

Department of Chemistry, Biochemistry and Biophysics, Gothenburg University, 40530 Gothenburg, Sweden. [email protected]