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Insights into how nucleotide-binding domains power ABC transport

DOI: 10.1016/j.str.2009.07.009 DOI Help
PMID: 19748342 PMID Help

Authors: Philip W. Fowler (University of Oxford) , Paul Bilton (University of Edinburgh) , Elizabeth P. Carpenter (Diamond Light Source) , Peter J. Sadler (University of Edinburgh) , Dominic J. Campopiano (University of Edinburgh) , Mark S. P. Sansom (University of Oxford) , So Iwata (Diamond Light Source) , Simon Newstead (Imperial College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Structure , VOL 17 (9) , PAGES 1213-22.

State: Published (Approved)
Published: September 2009
Diamond Proposal Number(s): 316

Open Access Open Access

Abstract: 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.

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Membrane Protein Laboratory (MPL)
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Added On: 12/04/2010 14:11

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