Insights into how nucleotide-binding domains power ABC transport
Newstead, Simon, Fowler, Philip W., Bilton, Paul R., Carpenter, Elisabeth P., Sadler, P. J., Campopiano, Dominic J., Sansom, M. S. P. (Mark S. P.) and Iwata, So. (2009) Insights into how nucleotide-binding domains power ABC transport. Structure, Vol.17 (NO.9). pp. 1213-1222. ISSN 0969-2126Full text not available from this repository.
Official URL: http://dx.doi.org/10.1016/j.str.2009.07.009
The mechanism by which nucleotide-binding domains (NBDs) of ABC transporters power the transport of substrates across cell membranes is currently unclear. Here we report the crystal structure of an NBD, FbpC, from the Neisseria gonorrhoeae ferric iron uptake transporter with an unusual and substantial domain swap in the C-terminal regulatory domain. This entanglement suggests that FbpC is unable to open to the same extent as the homologous protein MalK. Using molecular dynamics we demonstrate that this is not the case: both NBDs open rapidly once ATP is removed. We conclude from this result that the closed structures of FbpC and MalK have higher free energies than their respective open states. This result has important implications for our understanding of the mechanism of power generation in ABC transporters, because the unwinding of this free energy ensures that the opening of these two NBDs is also powered.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QP Physiology
|Divisions:||Faculty of Science > Chemistry|
|Library of Congress Subject Headings (LCSH):||ATP-binding cassette transporters, Hydrolysis|
|Journal or Publication Title:||Structure|
|Official Date:||9 September 2009|
|Page Range:||pp. 1213-1222|
|Access rights to Published version:||Restricted or Subscription Access|
|Funder:||Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Wellcome Trust (London, England), University of Edinburgh|
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