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| <StructureSection load='7n59' size='340' side='right'caption='[[7n59]], [[Resolution|resolution]] 3.60Å' scene=''> | | <StructureSection load='7n59' size='340' side='right'caption='[[7n59]], [[Resolution|resolution]] 3.60Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7n59]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N59 FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N59 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDS:OXIDIZED+GLUTATHIONE+DISULFIDE'>GDS</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> |
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDS:OXIDIZED+GLUTATHIONE+DISULFIDE'>GDS</scene></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=7n59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n59 OCA], [https://pdbe.org/7n59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n59 RCSB], [https://www.ebi.ac.uk/pdbsum/7n59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n59 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=7n59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n59 OCA], [https://pdbe.org/7n59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n59 RCSB], [https://www.ebi.ac.uk/pdbsum/7n59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n59 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function ==
| |
| [[https://www.uniprot.org/uniprot/AB25B_ARATH AB25B_ARATH]] Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins. Not required for mitochondrial and plastid Fe-S enzymes. Probably involved in the export of cyclic pyranopterin monophosphate (cPMP) from mitochondria into the cytosol. Mediates glutathione-dependent resistance to heavy metals such as cadmium and lead, as well as their transport from roots to leaves. Regulates nonprotein thiols (NPSH) and the cellular level of glutathione (GSH).<ref>PMID:11158531</ref> <ref>PMID:16461380</ref> <ref>PMID:17517886</ref> <ref>PMID:19710232</ref> <ref>PMID:20164445</ref>
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The ATP binding cassette (ABC) transporter of mitochondria (Atm) from Arabidopsis thaliana (AtAtm3) has been implicated in the maturation of cytosolic iron-sulfur proteins and heavy metal detoxification, plausibly by exporting glutathione derivatives. Using single-particle cryo-electron microscopy, we have determined four structures of AtAtm3 in three different conformational states: two inward-facing conformations (with and without bound oxidized glutathione [GSSG]), together with closed and outward-facing states stabilized by MgADP-VO4. These structures not only provide a structural framework for defining the alternating access transport cycle, but also reveal the paucity of cysteine residues in the glutathione binding site that could potentially form inhibitory mixed disulfides with GSSG. Despite extensive efforts, we were unable to prepare the ternary complex of AtAtm3 containing both GSSG and MgATP. A survey of structurally characterized type IV ABC transporters that includes AtAtm3 establishes that while nucleotides are found associated with all conformational states, they are effectively required to stabilize occluded, closed, and outward-facing conformations. In contrast, transport substrates have only been observed associated with inward-facing conformations. The absence of structures with dimerized nucleotide binding domains containing both nucleotide and transport substrate suggests that this form of the ternary complex exists only transiently during the transport cycle.
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| Glutathione binding to the plant AtAtm3 transporter and implications for the conformational coupling of ABC transporters.,Fan C, Rees DC Elife. 2022 Mar 25;11. pii: 76140. doi: 10.7554/eLife.76140. PMID:35333177<ref>PMID:35333177</ref>
| | ==See Also== |
| | | *[[ABC transporter 3D structures|ABC transporter 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7n59" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Fan, C]] | | [[Category: Fan C]] |
| [[Category: Rees, D C]] | | [[Category: Rees DC]] |
| [[Category: Atpase]]
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| [[Category: Membrane protein]]
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