- 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.
- Publication status:
- Published
- Publisher copy:
- 10.1016/j.febslet.2005.06.027
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- Journal:
- FEBS letters
- Volume:
- 579
- Issue:
- 19
- Pages:
- 4193-4199
- Publication date:
- 2005-08-05
- DOI:
- EISSN:
-
1873-3468
- ISSN:
-
0014-5793
- URN:
-
uuid:652f97bc-a9f7-4441-8d63-2ce6acd35672
- Source identifiers:
-
100840
- Local pid:
- pubs:100840
- Copyright date:
- 2005
Journal article
Nucleotide binding to the homodimeric MJ0796 protein: a computational study of a prokaryotic ABC transporter NBD dimer.
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