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Biophys. J. BioFAST: First Published January 5, 2007. doi:10.1529/biophysj.106.097972
© 2007 by the Biophysical Society.

A more recent version of this article appeared on April 15, 2007.
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CHANNELS, RECEPTORS, AND ELECTRICAL SIGNALING

SIMULATION OF THE COUPLING BETWEEN NUCLEOTIDE BINDING AND TRANSMEMBRANE DOMAINS IN THE ABC TRANSPORTER BtuCD

Jacob Sonne 1, Christian Kandt 2, Günther H. Peters 1, Flemming Y. 3, Morten Ø. Jensen 4 and D. Peter Tieleman 2*

1 Technical University of Denmark
2 University of Calgary
3 Hansen
4 Roskilde University

* To whom correspondence should be addressed. E-mail: tieleman{at}ucalgary.ca.

Submitted on September 22, 2006
Revised on October 22, 2006
Accepted on 11 December 2006


  Abstract
The nucleotide induced structural rearrangements in ABC transporters, leading to substrate translocation, are largely unknown. We have modeled nucleotide binding and release in the vitamin B12 importer BtuCD using perturbed elastic network calculations and biased molecular dynamics (MD) simulations. Both models predict that nucleotide release decreases the tilt between the two membrane spanning domains and opens the cytoplasmic gate. Nucleotide binding has the opposite effect. The observed coupling may be relevant for all ABC transporters, because of the conservation of nucleotide binding domains and the shared role of ATP in ABC transporters. The rearrangements in the cytoplasmic gate region do not provide enough space for B12 to diffuse from the transporter pore into the cytoplasm, which could suggest that peristaltic forces are needed to exclude B12 from the transporter pore.

Key Words: ABC transporter, ATPase, bacterial importer, computer simulation, normal mode analysis




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Copyright © 2007 by the Biophysical Society.