6roj
From Proteopedia
(Difference between revisions)
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<StructureSection load='6roj' size='340' side='right'caption='[[6roj]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='6roj' size='340' side='right'caption='[[6roj]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6roj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ROJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ROJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6roj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pneumoniae"_(schroeter_1886)_flugge_1886 "bacillus pneumoniae" (schroeter 1886) flugge 1886] and [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ROJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ROJ FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2Y5:(2R)-1-{[(R)-HYDROXY{[(1R,2R,3R,4R,5S,6R)-2,3,5,6-TETRAHYDROXY-4-(PHOSPHONOOXY)CYCLOHEXYL]OXY}PHOSPHORYL]OXY}-3-(OCTADECANOYLOXY)PROPAN-2-YL+(5Z,8Z,11Z,14Z)-ICOSA-5,8,11,14-TETRAENOATE'>2Y5</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2Y5:(2R)-1-{[(R)-HYDROXY{[(1R,2R,3R,4R,5S,6R)-2,3,5,6-TETRAHYDROXY-4-(PHOSPHONOOXY)CYCLOHEXYL]OXY}PHOSPHORYL]OXY}-3-(OCTADECANOYLOXY)PROPAN-2-YL+(5Z,8Z,11Z,14Z)-ICOSA-5,8,11,14-TETRAENOATE'>2Y5</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">oadA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=573 "Bacillus pneumoniae" (Schroeter 1886) Flugge 1886]), CDC50, YCR094W, YCR94W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6roj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6roj OCA], [http://pdbe.org/6roj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6roj RCSB], [http://www.ebi.ac.uk/pdbsum/6roj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6roj ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6roj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6roj OCA], [http://pdbe.org/6roj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6roj RCSB], [http://www.ebi.ac.uk/pdbsum/6roj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6roj 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. | [[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 == | ||
| + | Type 4 P-type ATPases (P4-ATPases) are lipid flippases that drive the active transport of phospholipids from exoplasmic or luminal leaflets to cytosolic leaflets of eukaryotic membranes. The molecular architecture of P4-ATPases and the mechanism through which they recognize and transport lipids have remained unknown. Here we describe the cryo-electron microscopy structure of the P4-ATPase Drs2p-Cdc50p, a Saccharomyces cerevisiae lipid flippase that is specific to phosphatidylserine and phosphatidylethanolamine. Drs2p-Cdc50p is autoinhibited by the C-terminal tail of Drs2p, and activated by the lipid phosphatidylinositol-4-phosphate (PtdIns4P or PI4P). We present three structures that represent the complex in an autoinhibited, an intermediate and a fully activated state. The analysis highlights specific features of P4-ATPases and reveals sites of autoinhibition and PI4P-dependent activation. We also observe a putative lipid translocation pathway in this flippase that involves a conserved PISL motif in transmembrane segment 4 and polar residues of transmembrane segments 2 and 5, in particular Lys1018, in the centre of the lipid bilayer. | ||
| + | |||
| + | Structure and autoregulation of a P4-ATPase lipid flippase.,Timcenko M, Lyons JA, Januliene D, Ulstrup JJ, Dieudonne T, Montigny C, Ash MR, Karlsen JL, Boesen T, Kuhlbrandt W, Lenoir G, Moeller A, Nissen P Nature. 2019 Jun 26. pii: 10.1038/s41586-019-1344-7. doi:, 10.1038/s41586-019-1344-7. PMID:31243363<ref>PMID:31243363</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6roj" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Baker's yeast]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ash, M R]] | [[Category: Ash, M R]] | ||
Revision as of 06:43, 10 July 2019
Cryo-EM structure of the activated Drs2p-Cdc50p
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