2C3E

The bovine mitochondrial ADP-ATP carrier

Summary for 2C3E

• Entry DOI: 10.2210/pdb2c3e/pdb
• Related: 1OKC
• Descriptor: ADP/ATP TRANSLOCASE 1, Carboxyatractyloside, CARDIOLIPIN (3 entities in total)
• Functional Keywords: mitochondrial carrier, nucleotide transport, membrane protein, transport protein
• Biological source: BOS TAURUS (CATTLE)
• Cellular location: Mitochondrion inner membrane; Multi-pass membrane protein: P02722
• Total number of polymer chains: 1
• Total formula weight: 38042.19

Authors

Nury, H.,Dahout-Gonzalez, C.,Trezeguet, V.,Lauquin, G.,Brandolin, G.,Pebay-Peyroula, E. (deposition date: 2005-10-06, release date: 2005-10-20, Last modification date: 2023-12-13)

Primary citation

Nury, H.,Dahout-Gonzalez, C.,Trezeguet, V.,Lauquin, G.,Brandolin, G.,Pebay-Peyroula, E.
Structural Basis for Lipid-Mediated Interactions between Mitochondrial Adp/ATP Carrier Monomers.
FEBS Lett., 579:6031-, 2005

PubMed Abstract: 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.

PubMed: 16226253
DOI: 10.1016/J.FEBSLET.2005.09.061

Experimental method

X-RAY DIFFRACTION (2.8 Å)