This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


6psx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: '''Unreleased structure''' The entry 6psx is ON HOLD Authors: Bai, L., Li, H. Description: Cryo-EM structure of S. cerevisiae Drs2p-Cdc50p in the PI4P-activated form [[Category: Unrele...)
Current revision (04:35, 11 April 2020) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 6psx is ON HOLD
+
==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 [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>
 +
</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='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='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'>[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>
 +
== 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.
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
Authors: Bai, L., Li, H.
+
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>
-
Description: Cryo-EM structure of S. cerevisiae Drs2p-Cdc50p in the PI4P-activated form
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
 +
<div class="pdbe-citations 6psx" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</SX>
 +
[[Category: Large Structures]]
 +
[[Category: P-type phospholipid transporter]]
 +
[[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]]

Current revision

Cryo-EM structure of S. cerevisiae Drs2p-Cdc50p in the PI4P-activated form

6psx, resolution 3.30Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools