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| | <StructureSection load='2c3e' size='340' side='right'caption='[[2c3e]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='2c3e' size='340' side='right'caption='[[2c3e]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2c3e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C3E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2c3e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C3E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=CXT:CARBOXYATRACTYLOSIDE'>CXT</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1okc|1okc]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=CXT:CARBOXYATRACTYLOSIDE'>CXT</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2c3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c3e RCSB], [http://www.ebi.ac.uk/pdbsum/2c3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c3e ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c3e OCA], [https://pdbe.org/2c3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c3e RCSB], [https://www.ebi.ac.uk/pdbsum/2c3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c3e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ADT1_BOVIN ADT1_BOVIN]] Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. | + | [https://www.uniprot.org/uniprot/ADT1_BOVIN ADT1_BOVIN] Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brandolin, G]] | + | [[Category: Brandolin G]] |
| - | [[Category: Dahout-Gonzalez, C]] | + | [[Category: Dahout-Gonzalez C]] |
| - | [[Category: Lauquin, G]] | + | [[Category: Lauquin G]] |
| - | [[Category: Nury, H]] | + | [[Category: Nury H]] |
| - | [[Category: Pebay-Peyroula, E]] | + | [[Category: Pebay-Peyroula E]] |
| - | [[Category: Trezeguet, V]] | + | [[Category: Trezeguet V]] |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Mitochondrial carrier]]
| + | |
| - | [[Category: Nucleotide transport]]
| + | |
| - | [[Category: Transport protein]]
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| Structural highlights
Function
ADT1_BOVIN Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2005 Nov 7;579(27):6031-6. Epub 2005 Oct 6. PMID:16226253 doi:10.1016/j.febslet.2005.09.061
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