Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers

The oligomerization state of the ADP/ATP carrier is an important issue in understanding the mechanism underlying nucleotide exchange across the inner mitochondrial membrane. The first high resolution structure obtained in the presence of carboxyatractyloside revealed a large cavity formed within a monomer in which the inhibitor is strongly bound. Whereas the protein-protein interactions implicated in the first crystal form are not biologically relevant, the new crystal form described herein, highlights favorable protein-protein interactions. The interactions are mediated by endogenous cardiolipins, which are tightly bound to the protein, two cardiolipins being sandwiched between the monomers on the matrix side. The putative dimerization interface evidenced here is consistent with other structural, biochemical or functional data published so far.


Published in:
FEBS letters, 579, 27, 6031-6
Year:
2005
Publisher:
Elsevier
ISSN:
0014-5793
Laboratories:




 Record created 2010-10-11, last modified 2018-03-17


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