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Nucleotide binding to the homodimeric MJ0796 protein: A computational study of a prokaryotic ABC transporter NBD dimer
Author(s) -
Campbell Jeff D.,
Sansom Mark S.P.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.06.027
Subject(s) - atp binding cassette transporter , nucleotide , dimer , chemistry , transporter , adenosine triphosphate , plasma protein binding , binding site , biophysics , biochemistry , biology , gene , organic chemistry
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.