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4exv

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==Structure of Kluyveromyces lactis Hsv2p==
==Structure of Kluyveromyces lactis Hsv2p==
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<StructureSection load='4exv' size='340' side='right' caption='[[4exv]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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<StructureSection load='4exv' size='340' side='right'caption='[[4exv]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4exv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EXV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EXV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4exv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis_NRRL_Y-1140 Kluyveromyces lactis NRRL Y-1140]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EXV FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSV2, KLLA0E15972g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28985 Kluyveromyces lactis])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=4exv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4exv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4exv RCSB], [http://www.ebi.ac.uk/pdbsum/4exv PDBsum]</span></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=4exv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4exv OCA], [https://pdbe.org/4exv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4exv RCSB], [https://www.ebi.ac.uk/pdbsum/4exv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4exv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HSV2_KLULA HSV2_KLULA]] Involved in mitochondrial or peroxisomal functions and amino acid signaling pathways (By similarity).
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[https://www.uniprot.org/uniprot/HSV2_KLULA HSV2_KLULA] Involved in mitochondrial or peroxisomal functions and amino acid signaling pathways (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Macroautophagy is essential to cell survival during starvation and proceeds by the growth of a double-membraned phagophore, which engulfs cytosol and other substrates. The synthesis and recognition of the lipid phosphatidylinositol 3-phosphate, PI(3)P, is essential for autophagy. The key autophagic PI(3)P sensors, which are conserved from yeast to humans, belong to the PROPPIN family. Here we report the crystal structure of the yeast PROPPIN Hsv2. The structure consists of a seven-bladed beta-propeller and, unexpectedly, contains two pseudo-equivalent PI(3)P binding sites on blades 5 and 6. These two sites both contribute to membrane binding in vitro and are collectively required for full autophagic function in yeast. These sites function in concert with membrane binding by a hydrophobic loop in blade 6, explaining the specificity of the PROPPINs for membrane-bound PI(3)P. These observations thus provide a structural and mechanistic framework for one of the conserved central molecular recognition events in autophagy.
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Two-Site Recognition of Phosphatidylinositol 3-Phosphate by PROPPINs in Autophagy.,Baskaran S, Ragusa MJ, Boura E, Hurley JH Mol Cell. 2012 Jun 14. PMID:22704557<ref>PMID:22704557</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Kluyveromyces lactis]]
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[[Category: Kluyveromyces lactis NRRL Y-1140]]
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[[Category: Baskaran, S]]
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[[Category: Large Structures]]
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[[Category: Hurley, J H]]
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[[Category: Baskaran S]]
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[[Category: Atg2]]
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[[Category: Hurley JH]]
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[[Category: Atg21]]
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[[Category: Atg9]]
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[[Category: Autophagy]]
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[[Category: Phosphate binding]]
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[[Category: Phosphatidylinositol]]
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[[Category: Phosphoinoside]]
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[[Category: Proppin]]
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[[Category: Transport protein]]
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[[Category: Wd-repeat]]
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Current revision

Structure of Kluyveromyces lactis Hsv2p

PDB ID 4exv

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