2c3e
From Proteopedia
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==Overview== | ==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 . | + | 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== | ==About this Structure== | ||
| - | 2C3E is a | + | 2C3E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CXT and CDL as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C3E OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:47:55 2007'' |
Revision as of 11:42, 5 November 2007
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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 with CXT and CDL as ligands. Structure known Active Site: AC1. 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
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