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| | <SX load='6psx' size='340' side='right' viewer='molstar' caption='[[6psx]], [[Resolution|resolution]] 3.30Å' scene=''> | | <SX load='6psx' size='340' side='right' viewer='molstar' caption='[[6psx]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6psx]] is a 2 chain structure with sequence from [http://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 [http://proteopedia.org/fgij/fg.htm?mol=6PSX FirstGlance]. <br> | + | <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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DRS2, YAL026C, FUN38 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=580240 Saccharomyces cerevisiae W303]), CDC50, YCR094W, YCR94W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=580240 Saccharomyces cerevisiae W303])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/P-type_phospholipid_transporter P-type phospholipid transporter], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=7.6.2.1 7.6.2.1] </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=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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6psx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6psx OCA], [http://pdbe.org/6psx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6psx RCSB], [http://www.ebi.ac.uk/pdbsum/6psx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6psx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. [[http://www.uniprot.org/uniprot/CDC50_YEAST CDC50_YEAST]] Required for polarized cell growth. | + | [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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: P-type phospholipid transporter]]
| + | [[Category: Saccharomyces cerevisiae W303]] |
| - | [[Category: Saccharomyces cerevisiae w303]] | + | [[Category: Bai L]] |
| - | [[Category: Bai, L]] | + | [[Category: Li H]] |
| - | [[Category: Li, H]] | + | |
| - | [[Category: Complex]]
| + | |
| - | [[Category: P-type atpase]]
| + | |
| - | [[Category: Phospholipid flippase]]
| + | |
| - | [[Category: Translocase]]
| + | |
| Structural highlights
Function
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bai L, Kovach A, You Q, Hsu HC, Zhao G, Li H. Autoinhibition and activation mechanisms of the eukaryotic lipid flippase Drs2p-Cdc50p. Nat Commun. 2019 Sep 12;10(1):4142. doi: 10.1038/s41467-019-12191-9. PMID:31515475 doi:http://dx.doi.org/10.1038/s41467-019-12191-9
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