5jys

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'''Unreleased structure'''
 
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The entry 5jys is ON HOLD
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==Pry1 CAP domain==
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<StructureSection load='5jys' size='340' side='right'caption='[[5jys]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5jys]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JYS FirstGlance]. <br>
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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]] 1.901&#8491;</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=MG:MAGNESIUM+ION'>MG</scene></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=5jys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jys OCA], [https://pdbe.org/5jys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jys RCSB], [https://www.ebi.ac.uk/pdbsum/5jys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jys ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PRY1_YEAST PRY1_YEAST] Secreted protein required for efficient export of lipids such as acetylated sterols. Acts in detoxification of hydrophobic compounds.<ref>PMID:23027975</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The production, crystal structure, and functional characterization of the C-terminal cysteine-rich secretory protein/antigen 5/pathogenesis related-1 (CAP) domain of pathogen-related yeast protein-1 (Pry1) from Saccharomyces cerevisiae is presented. The CAP domain of Pry1 (Pry1CAP) is functional in vivo as its expression restores cholesterol export to yeast mutants lacking endogenous Pry1 and Pry2. Recombinant Pry1CAP forms dimers in solution, is sufficient for in vitro cholesterol binding, and has comparable binding properties as full-length Pry1. Two crystal structures of Pry1CAP are reported, one with Mg(2+) coordinated to the conserved CAP tetrad (His208, Glu215, Glu233 and His250) in spacegroup I41 and the other without divalent cations in spacegroup P6122. The latter structure contains four 1,4-dioxane molecules from the crystallization solution, one of which sits in the cholesterol binding site. Both structures reveal that the divalent cation and cholesterol binding sites are connected upon dimerization, providing a structural basis for the observed Mg(2+)-dependent sterol binding by Pry1.
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Authors: Asojo, O.A.
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Structural and functional characterization of the CAP domain of pathogen-related yeast 1 (Pry1) protein.,Darwiche R, Kelleher A, Hudspeth EM, Schneiter R, Asojo OA Sci Rep. 2016 Jun 27;6:28838. doi: 10.1038/srep28838. PMID:27344972<ref>PMID:27344972</ref>
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Description: Pry1 CAP domain
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Asojo, O.A]]
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<div class="pdbe-citations 5jys" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Asojo OA]]

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Pry1 CAP domain

PDB ID 5jys

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