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4c9q

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<StructureSection load='4c9q' size='340' side='right'caption='[[4c9q]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='4c9q' size='340' side='right'caption='[[4c9q]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4c9q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C9Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4c9q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C9Q FirstGlance]. <br>
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</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>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c9g|4c9g]], [[4c9h|4c9h]], [[4c9j|4c9j]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9q OCA], [https://pdbe.org/4c9q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c9q RCSB], [https://www.ebi.ac.uk/pdbsum/4c9q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c9q ProSAT]</span></td></tr>
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<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=4c9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9q OCA], [http://pdbe.org/4c9q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c9q RCSB], [http://www.ebi.ac.uk/pdbsum/4c9q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c9q ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ADT3_YEAST ADT3_YEAST]] Catalyzes the exchange of ADP and ATP across the mitochondrial inner membrane.
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[[https://www.uniprot.org/uniprot/ADT3_YEAST ADT3_YEAST]] Catalyzes the exchange of ADP and ATP across the mitochondrial inner membrane.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The mitochondrial ADP/ATP carrier imports ADP from the cytosol and exports ATP from the mitochondrial matrix. The carrier cycles by an unresolved mechanism between the cytoplasmic state, in which the carrier accepts ADP from the cytoplasm, and the matrix state, in which it accepts ATP from the mitochondrial matrix. Here we present the structures of the yeast ADP/ATP carriers Aac2p and Aac3p in the cytoplasmic state. The carriers have three domains and are closed at the matrix side by three interdomain salt-bridge interactions, one of which is braced by a glutamine residue. Glutamine braces are conserved in mitochondrial carriers and contribute to an energy barrier, preventing the conversion to the matrix state unless substrate binding occurs. At the cytoplasmic side a second salt-bridge network forms during the transport cycle, as demonstrated by functional analysis of mutants with charge-reversed networks. Analyses of the domain structures and properties of the interdomain interfaces indicate that interconversion between states involves movement of the even-numbered alpha-helices across the surfaces of the odd-numbered alpha-helices by rotation of the domains. The odd-numbered alpha-helices have an L-shape, with proline or serine residues at the kinks, which functions as a lever-arm, coupling the substrate-induced disruption of the matrix network to the formation of the cytoplasmic network. The simultaneous movement of three domains around a central translocation pathway constitutes a unique mechanism among transport proteins. These findings provide a structural description of transport by mitochondrial carrier proteins, consistent with an alternating-access mechanism.
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Structures of yeast mitochondrial ADP/ATP carriers support a domain-based alternating-access transport mechanism.,Ruprecht JJ, Hellawell AM, Harding M, Crichton PG, McCoy AJ, Kunji ER Proc Natl Acad Sci U S A. 2014 Jan 28;111(4):E426-34. doi:, 10.1073/pnas.1320692111. Epub 2014 Jan 13. PMID:24474793<ref>PMID:24474793</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4c9q" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 18824]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Crichton, P G]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Harding, M]]
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[[Category: Crichton PG]]
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[[Category: Hellawell, A M]]
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[[Category: Harding M]]
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[[Category: Kunji, E R.S]]
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[[Category: Hellawell AM]]
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[[Category: McCoy, A J]]
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[[Category: Kunji ERS]]
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[[Category: Ruprecht, J J]]
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[[Category: McCoy AJ]]
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[[Category: Adp/atp carrier]]
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[[Category: Ruprecht JJ]]
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[[Category: Mitochondrial carrier]]
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[[Category: Transport protein]]
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Revision as of 17:33, 7 September 2022

Structure of yeast mitochondrial ADP/ATP carrier isoform 3 inhibited by carboxyatractyloside (P21 crystal form)

PDB ID 4c9q

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