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Crystal Structure of AcrB in Complex with a Single Transmembrane Subunit Reveals Another Twist.

Susanna Törnroth-Horsefield ; Pontus Gourdon (Institutionen för kemi- och bioteknik, Molekylär bioteknik) ; Rob Horsefield ; Lars Brive ; Natsuko Yamamoto ; Hirotada Mori ; Arjan Snijder (Institutionen för kemi- och bioteknik, Molekylär bioteknik) ; Richard Neutze
Structure (London, England : 1993) (0969-2126). Vol. 15 (2007), 12, p. 1663-73.
[Artikel, refereegranskad vetenskaplig]

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.

Nyckelord: PROTEINS

Denna post skapades 2008-01-10. Senast ändrad 2011-01-20.
CPL Pubid: 65378


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Institutioner (Chalmers)

Institutionen för kemi (2001-2011)
Institutionen för kemi- och bioteknik, Molekylär bioteknik (2005-2007)
Institutionen för cell- och molekylärbiologi (1994-2011)


Bioinformatik och systembiologi

Chalmers infrastruktur