2c3e
From Proteopedia
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| , resolution 2.8Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE BOVINE MITOCHONDRIAL ADP-ATP CARRIER
Overview
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.
About this Structure
2C3E is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers., Nury H, Dahout-Gonzalez C, Trezeguet V, Lauquin G, Brandolin G, Pebay-Peyroula E, FEBS Lett. 2005 Nov 7;579(27):6031-6. Epub 2005 Oct 6. PMID:16226253
Page seeded by OCA on Mon Mar 31 02:15:42 2008
