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Transport by ABC proteins requires a cycle of ATP-driven conformational changes of the nucleotide binding domains (NBDs). We compare three molecular dynamics simulations of dimeric MJ0796: with ATP was present at both NBDs; with ATP at one NBD but ADP at the other; and without any bound ATP. In the simulation with ATP present at both NBDs, the dimeric protein interacts with the nucleotides in a symmetrical manner. However, if ADP is present at one binding site then both NBD-NBD and protein-ATP interactions are enhanced at the opposite site.

Original publication

DOI

10.1016/j.febslet.2005.06.027

Type

Journal article

Journal

FEBS Lett

Publication Date

01/08/2005

Volume

579

Pages

4193 - 4199

Keywords

ATP-Binding Cassette Transporters, Adenosine Diphosphate, Adenosine Triphosphate, Binding Sites, Computational Biology, Crystallography, X-Ray, Dimerization, Models, Molecular, Protein Binding, Protein Conformation