title: Nucleotide binding to the homodimeric MJ0796 protein: a computational study of a prokaryotic ABC transporter NBD dimer.
abstract: 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.
authors.affiliation: Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
authors.forename: Jeff D
authors.initials: JD
authors.lastname: Campbell
authors.forename: Mark S P
authors.initials: MS
authors.lastname: Sansom
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000737:chemistry / Q000378:metabolism*; D000244:Adenosine Diphosphate / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D001665:Binding Sites; D019295:Computational Biology; D018360:Crystallography, X-Ray; D019281:Dimerization; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D018528:ATP-Binding Cassette Transporters; C434961:MJ0796 protein, Methanococcus jannaschii; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate