3plt

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<StructureSection load='3plt' size='340' side='right'caption='[[3plt]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='3plt' size='340' side='right'caption='[[3plt]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3plt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PLT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3plt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PLT FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3kq1|3kq1]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LSP1, YPL004C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3plt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3plt OCA], [https://pdbe.org/3plt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3plt RCSB], [https://www.ebi.ac.uk/pdbsum/3plt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3plt ProSAT]</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=3plt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3plt OCA], [https://pdbe.org/3plt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3plt RCSB], [https://www.ebi.ac.uk/pdbsum/3plt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3plt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/LSP1_YEAST LSP1_YEAST]] Together with PIL1, main component of eisosomes, structures at the cell periphery underneath the plasma membrane that mark the site of endocytosis. Negative regulator of cell wall integrity (CWI) in unstressed cells, probably by inhibiting protein kinase PKH1/PHK2 activity and regulating their downstream CWI pathways PKC1-MAP kinase pathway and protein kinase YPK1 pathway. Activity may be regulated by the transient increase of sphingolipid long chain bases (LCBs) during heat stress.<ref>PMID:15016821</ref>
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[https://www.uniprot.org/uniprot/LSP1_YEAST LSP1_YEAST] Together with PIL1, main component of eisosomes, structures at the cell periphery underneath the plasma membrane that mark the site of endocytosis. Negative regulator of cell wall integrity (CWI) in unstressed cells, probably by inhibiting protein kinase PKH1/PHK2 activity and regulating their downstream CWI pathways PKC1-MAP kinase pathway and protein kinase YPK1 pathway. Activity may be regulated by the transient increase of sphingolipid long chain bases (LCBs) during heat stress.<ref>PMID:15016821</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Plasma membranes are organized into domains of different protein and lipid composition. Eisosomes are key complexes for yeast plasma membrane organization, containing primarily Pil1 and Lsp1. Here we show that both proteins consist mostly of a banana-shaped BAR domain common to membrane sculpting proteins, most similar to the ones of amphiphysin, arfaptin 2 and endophilin 2. Our data reveal a previously unrecognized family of BAR-domain proteins involved in plasma membrane organization.
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Eisosome-driven plasma membrane organization is mediated by BAR domains.,Ziolkowska NE, Karotki L, Rehman M, Huiskonen JT, Walther TC Nat Struct Mol Biol. 2011 Jun 19. doi: 10.1038/nsmb.2080. PMID:21685922<ref>PMID:21685922</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3plt" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 18824]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Walther, T C]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Ziolkowska, N E]]
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[[Category: Walther TC]]
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[[Category: Bar domain]]
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[[Category: Ziolkowska NE]]
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[[Category: Eisosome]]
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[[Category: Lsp1]]
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[[Category: Phosphoprotein]]
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[[Category: Pil1]]
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[[Category: Plasma membrane]]
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[[Category: Self-assembly]]
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[[Category: Structural protein]]
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Current revision

Crystal structure of Lsp1 from Saccharomyces cerevisiae

PDB ID 3plt

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