7op8
From Proteopedia
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<StructureSection load='7op8' size='340' side='right'caption='[[7op8]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='7op8' size='340' side='right'caption='[[7op8]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OP8 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</td></tr> |
| - | <tr id=' | + | <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=MG:MAGNESIUM+ION'>MG</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=7op8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7op8 OCA], [https://pdbe.org/7op8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7op8 RCSB], [https://www.ebi.ac.uk/pdbsum/7op8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7op8 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=7op8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7op8 OCA], [https://pdbe.org/7op8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7op8 RCSB], [https://www.ebi.ac.uk/pdbsum/7op8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7op8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | In human cells, P5B-ATPases execute the active export of physiologically important polyamines such as spermine from lysosomes to the cytosol, a function linked to a palette of disorders. Yet, the overall shape of P5B-ATPases and the mechanisms of polyamine recognition, uptake and transport remain elusive. Here we describe a series of cryo-electron microscopy structures of a yeast homolog of human ATP13A2-5, Ypk9, determined at resolutions reaching 3.4 A, and depicting three separate transport cycle intermediates, including spermine-bound conformations. Surprisingly, in the absence of cargo, Ypk9 rests in a phosphorylated conformation auto-inhibited by the N-terminus. Spermine uptake is accomplished through an electronegative cleft lined by transmembrane segments 2, 4 and 6. Despite the dramatically different nature of the transported cargo, these findings pinpoint shared principles of transport and regulation among the evolutionary related P4-, P5A- and P5B-ATPases. The data also provide a framework for analysis of associated maladies, such as Parkinson's disease. | ||
| - | + | ==See Also== | |
| - | + | *[[ATPase 3D structures|ATPase 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Chatd]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Ping L]] |
| - | [[Category: Pontus | + | [[Category: Pontus G]] |
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Current revision
Cryo-EM structure of P5B-ATPase E2Pinhibit
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