Dynamics of the trimeric AcrB transporter protein inferred from a B-factor analysis of the crystal structure.
The Escherichia coli AcrB multidrug transporter recognizes a wide range of toxic chemicals and actively extrudes them from cells. The molecular basis of multidrug transport in AcrB remains unknown. Herein, we describe normal mode analyses to study important regions for drug recognition and extrusion in this transporter. Based on the X-ray structure of AcrB, an elastic network model has been able to correct errors arising from crystal imperfection in the experimental B-factors. The results allow us to understand the functional dynamics of this membrane protein. It is expected that this technique can be applied to other membrane proteins with known structures.
Lu
W C
WC
Ames Laboratory-U.S. DOE, Department of Physics and Astronomy, Iowa State University, Ames, Iowa 50011, USA.
Wang
C Z
CZ
Yu
E W
EW
Ho
K M
KM
D003461:Crystallography; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D046911:Macromolecular Substances / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry; D008958:Models, Molecular; D027425:ATP-Binding Cassette, Sub-Family C Proteins / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation
D029968:Escherichia coli Proteins; D046911:Macromolecular Substances; D008565:Membrane Proteins; D027425:ATP-Binding Cassette, Sub-Family C Proteins; C083496:AcrB protein, E coli