6gci

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Current revision (12:33, 16 January 2019) (edit) (undo)
 
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<StructureSection load='6gci' size='340' side='right' caption='[[6gci]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='6gci' size='340' side='right' caption='[[6gci]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6gci]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GCI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GCI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6gci]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Camelus_glama Camelus glama] and [http://en.wikipedia.org/wiki/Myctt Myctt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GCI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GCI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BKC:Bongkrekic+acid'>BKC</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BKC:Bongkrekic+acid'>BKC</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYCTH_2316753 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=573729 MYCTT])</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=6gci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gci OCA], [http://pdbe.org/6gci PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gci RCSB], [http://www.ebi.ac.uk/pdbsum/6gci PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gci ProSAT]</span></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=6gci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gci OCA], [http://pdbe.org/6gci PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gci RCSB], [http://www.ebi.ac.uk/pdbsum/6gci PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gci ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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The mitochondrial ADP/ATP carrier catalyses the equimolar exchange of adenosine di- and tri-phosphates. It operates by an alternating access mechanism in which a single substrate-binding site is made available either to the mitochondrial matrix or the intermembrane space through conformational changes. These changes are prevented in the absence of substrate by a large energy barrier due to the need for sequential disruption and formation of a matrix and cytoplasmic salt bridge network that are located on either side of the central cavity. In analogy to enzyme catalysis, substrate lowers the energy barrier by binding tighter in the intermediate state. Here we provide an in-silico kinetic model that captures the free energy profile of these conformational changes and treats the carrier as a nanomachine moving stochastically from the matrix to cytoplasmic conformation under the influence of thermal energy. The model reproduces the dependency of experimentally determined kcat and KM values on the cytoplasmic network strength with good quantitative accuracy, implying that it captures the transport mechanism and can provide a framework to understand the structure-function relationships of this class of transporter. The results show that maximum transport occurs when the interaction energies of the cytoplasmic network, matrix network and substrate binding are approximately equal such that the energy barrier is minimized. Consequently, the model predicts that there will be other interactions in addition to those of the cytoplasmic network that stabilise the matrix conformation of the ADP/ATP carrier.
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Mitochondrial ADP/ATP carriers transport ADP into the mitochondrial matrix for ATP synthesis, and ATP out to fuel the cell, by cycling between cytoplasmic-open and matrix-open states. The structure of the cytoplasmic-open state is known, but it has proved difficult to understand the transport mechanism in the absence of a structure in the matrix-open state. Here, we describe the structure of the matrix-open state locked by bongkrekic acid bound in the ADP/ATP-binding site at the bottom of the central cavity. The cytoplasmic side of the carrier is closed by conserved hydrophobic residues, and a salt bridge network, braced by tyrosines. Glycine and small amino acid residues allow close-packing of helices on the matrix side. Uniquely, the carrier switches between states by rotation of its three domains about a fulcrum provided by the substrate-binding site. Because these features are highly conserved, this mechanism is likely to apply to the whole mitochondrial carrier family.
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Modelling the free energy profile of the mitochondrial ADP/ATP carrier.,Springett R, King MS, Crichton PG, Kunji ERS Biochim Biophys Acta Bioenerg. 2017 Nov;1858(11):906-914. doi:, 10.1016/j.bbabio.2017.05.006. Epub 2017 May 26. PMID:28554566<ref>PMID:28554566</ref>
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The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier.,Ruprecht JJ, King MS, Zogg T, Aleksandrova AA, Pardon E, Crichton PG, Steyaert J, Kunji ERS Cell. 2019 Jan 2. pii: S0092-8674(18)31517-4. doi: 10.1016/j.cell.2018.11.025. PMID:30611538<ref>PMID:30611538</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Camelus glama]]
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[[Category: Myctt]]
[[Category: Aleksandrova, A A]]
[[Category: Aleksandrova, A A]]
[[Category: Crichton, P G]]
[[Category: Crichton, P G]]

Current revision

Structure of the bongkrekic acid-inhibited mitochondrial ADP/ATP carrier

6gci, resolution 3.30Å

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