7op8: Difference between revisions
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==Cryo-EM structure of P5B-ATPase E2Pinhibit== | ==Cryo-EM structure of P5B-ATPase E2Pinhibit== | ||
<StructureSection load='7op8' size='340' side='right'caption='[[7op8]]' scene=''> | <StructureSection load='7op8' size='340' side='right'caption='[[7op8]], [[Resolution|resolution]] 3.50Å' 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=7OP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OP8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7op8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chatd Chatd]. 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='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> | </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=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0028100 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD])</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. | |||
Structure and transport mechanism of P5B-ATPases.,Li P, Wang K, Salustros N, Gronberg C, Gourdon P Nat Commun. 2021 Jun 25;12(1):3973. doi: 10.1038/s41467-021-24148-y. PMID:34172751<ref>PMID:34172751</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7op8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Chatd]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Li, P]] | ||
[[Category: Pontus G]] | [[Category: Pontus, G]] | ||
[[Category: Spm transporter]] | |||
[[Category: Transport protein]] | |||
Revision as of 13:19, 7 July 2021
Cryo-EM structure of P5B-ATPase E2PinhibitCryo-EM structure of P5B-ATPase E2Pinhibit
Structural highlights
Publication Abstract from PubMedIn 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. Structure and transport mechanism of P5B-ATPases.,Li P, Wang K, Salustros N, Gronberg C, Gourdon P Nat Commun. 2021 Jun 25;12(1):3973. doi: 10.1038/s41467-021-24148-y. PMID:34172751[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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