6gci: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 6gci is ~~ON HOLD until Paper~~ Publication

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

== Structural highlights ==

<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>

<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>

</table>

== Publication Abstract from PubMed ==

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.

~~Authors~~:

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Camelus glama]]

[[Category: Myctt]]

[[Category: Aleksandrova, A A]]

[[Category: Crichton, P G]]

[[Category: King, M S]]

[[Category: Kunji, E R.S]]

[[Category: Pardon, E]]

[[Category: Ruprecht, J J]]

[[Category: Steyaert, J]]

[[Category: Zogg, T]]

[[Category: Carrier]]

[[Category: Inhibitor]]

[[Category: Membrane protein]]

[[Category: Mitochondrial]]

[[Category: Transporter]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6gci is ON HOLD  until Paper Publication
+==Structure of the bongkrekic acid-inhibited mitochondrial ADP/ATP carrier==
+<StructureSection load='6gci' size='340' side='right' caption='[[6gci]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
+== Structural highlights ==
+<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>
+<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>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6gci" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Camelus glama]]
+[[Category: Myctt]]
+[[Category: Aleksandrova, A A]]
+[[Category: Crichton, P G]]
+[[Category: King, M S]]
+[[Category: Kunji, E R.S]]
+[[Category: Pardon, E]]
+[[Category: Ruprecht, J J]]
+[[Category: Steyaert, J]]
+[[Category: Zogg, T]]
+[[Category: Carrier]]
+[[Category: Inhibitor]]
+[[Category: Membrane protein]]
+[[Category: Mitochondrial]]
+[[Category: Transporter]]