View source for 6psx


==Cryo-EM structure of S. cerevisiae Drs2p-Cdc50p in the PI4P-activated form==
<SX load='6psx' size='340' side='right' viewer='molstar' caption='[[6psx]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6psx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_W303 Saccharomyces cerevisiae W303]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PSX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=6psx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6psx OCA], [https://pdbe.org/6psx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6psx RCSB], [https://www.ebi.ac.uk/pdbsum/6psx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6psx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATC3_YEAST ATC3_YEAST] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (Potential). Seems to be involved in ribosome assembly.
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== Publication Abstract from PubMed ==
The heterodimeric eukaryotic Drs2p-Cdc50p complex is a lipid flippase that maintains cell membrane asymmetry. The enzyme complex exists in an autoinhibited form in the absence of an activator and is specifically activated by phosphatidylinositol-4-phosphate (PI4P), although the underlying mechanisms have been unclear. Here we report the cryo-EM structures of intact Drs2p-Cdc50p isolated from S. cerevisiae in apo form and in the PI4P-activated form at 2.8 A and 3.3 A resolution, respectively. The structures reveal that the Drs2p C-terminus lines a long groove in the cytosolic regulatory region to inhibit the flippase activity. PIP4 binding in a cytosol-proximal membrane region triggers a 90 degrees rotation of a cytosolic helix switch that is located just upstream of the inhibitory C-terminal peptide. The rotation of the helix switch dislodges the C-terminus from the regulatory region, activating the flippase.

Autoinhibition and activation mechanisms of the eukaryotic lipid flippase Drs2p-Cdc50p.,Bai L, Kovach A, You Q, Hsu HC, Zhao G, Li H Nat Commun. 2019 Sep 12;10(1):4142. doi: 10.1038/s41467-019-12191-9. PMID:31515475<ref>PMID:31515475</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6psx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</SX>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae W303]]
[[Category: Bai L]]
[[Category: Li H]]