2rdd
From Proteopedia
X-ray crystal structure of AcrB in complex with a novel transmembrane helix.
Overview
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.
About this Structure
2RDD is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of AcrB in complex with a single transmembrane subunit reveals another twist., Tornroth-Horsefield S, Gourdon P, Horsefield R, Brive L, Yamamoto N, Mori H, Snijder A, Neutze R, Structure. 2007 Dec;15(12):1663-73. PMID:18073115 Page seeded by OCA on Wed Apr 16 23:07:57 2008
Categories: Escherichia coli | Protein complex | Gourdon, P. | Horsefield, R. | Neutze, R. | Tornroth-Horsefield, S. | Acrb | Antiporter | Drug resistance | Inner membrane | Membrane protein | Membrane protein/transport protein complex | Multidrug efflux | Novel transmembrane helix | Transporter | Yajc
