2c3e

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[[Image:2c3e.gif|left|200px]]
[[Image:2c3e.gif|left|200px]]
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{{Structure
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|PDB= 2c3e |SIZE=350|CAPTION= <scene name='initialview01'>2c3e</scene>, resolution 2.8&Aring;
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|SITE= <scene name='pdbsite=AC1:Cdl+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=CXT:CARBOXYATRACTYLOSIDE'>CXT</scene>
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{{STRUCTURE_2c3e| PDB=2c3e | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c3e OCA], [http://www.ebi.ac.uk/pdbsum/2c3e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c3e RCSB]</span>
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'''THE BOVINE MITOCHONDRIAL ADP-ATP CARRIER'''
'''THE BOVINE MITOCHONDRIAL ADP-ATP CARRIER'''
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[[Category: Pebay-Peyroula, E.]]
[[Category: Pebay-Peyroula, E.]]
[[Category: Trezeguet, V.]]
[[Category: Trezeguet, V.]]
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[[Category: membrane protein]]
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[[Category: Membrane protein]]
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[[Category: mitochondrial carrier]]
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[[Category: Mitochondrial carrier]]
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[[Category: nucleotide transport]]
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[[Category: Nucleotide transport]]
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[[Category: transport protein]]
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[[Category: Transport protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:11:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:15:42 2008''
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Revision as of 18:11, 3 May 2008

Template:STRUCTURE 2c3e

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 Sat May 3 21:11:14 2008

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