7m5x
From Proteopedia
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| ==Transport protein in inhibited state 1== | ==Transport protein in inhibited state 1== | ||
| - | <StructureSection load='7m5x' size='340' side='right'caption='[[7m5x]]' scene=''> | + | <StructureSection load='7m5x' size='340' side='right'caption='[[7m5x]], [[Resolution|resolution]] 2.70Å' scene=''> | 
| == Structural highlights == | == Structural highlights == | ||
| <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7M5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M5X FirstGlance]. <br> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7M5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M5X FirstGlance]. <br> | ||
| - | </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=7m5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m5x OCA], [https://pdbe.org/7m5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m5x RCSB], [https://www.ebi.ac.uk/pdbsum/7m5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m5x ProSAT]</span></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]] 2.7Å</td></tr> | 
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=C14:TETRADECANE'>C14</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=D12:DODECANE'>D12</scene>, <scene name='pdbligand=EUJ:(2R)-3-{[(S)-hydroxy{[(1S,2R,3R,4S,5S,6R)-2,4,6-trihydroxy-3,5-bis(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}propane-1,2-diyl+dioctanoate'>EUJ</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SPK:SPERMINE+(FULLY+PROTONATED+FORM)'>SPK</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</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=7m5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m5x OCA], [https://pdbe.org/7m5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m5x RCSB], [https://www.ebi.ac.uk/pdbsum/7m5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m5x ProSAT]</span></td></tr> | ||
| </table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mutations in ATP13A2, also known as PARK9, cause a rare monogenic form of juvenile-onset Parkinson's disease named Kufor-Rakeb syndrome and other neurodegenerative diseases. ATP13A2 encodes a neuroprotective P5B P-type ATPase highly enriched in the brain that mediates selective import of spermine ions from lysosomes into the cytosol via an unknown mechanism. Here we present three structures of human ATP13A2 bound to an ATP analog or to spermine in the presence of phosphomimetics determined by cryoelectron microscopy. ATP13A2 autophosphorylation opens a lysosome luminal gate to reveal a narrow lumen access channel that holds a spermine ion in its entrance. ATP13A2's architecture suggests physical principles underlying selective polyamine transport and anticipates a "pump-channel" intermediate that could function as a counter-cation conduit to facilitate lysosome acidification. Our findings establish a firm foundation to understand ATP13A2 mutations associated with disease and bring us closer to realizing ATP13A2's potential in neuroprotective therapy. | ||
| + | |||
| + | Structural mechanisms for gating and ion selectivity of the human polyamine transporter ATP13A2.,Tillinghast J, Drury S, Bowser D, Benn A, Lee KPK Mol Cell. 2021 Nov 18;81(22):4650-4662.e4. doi: 10.1016/j.molcel.2021.10.002., Epub 2021 Oct 28. PMID:34715014<ref>PMID:34715014</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7m5x" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| __TOC__ | __TOC__ | ||
| </StructureSection> | </StructureSection> | ||
| [[Category: Large Structures]] | [[Category: Large Structures]] | ||
| [[Category: Lee KPK]] | [[Category: Lee KPK]] | ||
Current revision
Transport protein in inhibited state 1
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