1o6u

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(New page: 200px<br /> <applet load="1o6u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o6u, resolution 2.05&Aring;" /> '''THE CRYSTAL STRUCTU...)
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[[Image:1o6u.gif|left|200px]]<br />
 
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<applet load="1o6u" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1o6u, resolution 2.05&Aring;" />
 
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'''THE CRYSTAL STRUCTURE OF HUMAN SUPERNATANT PROTEIN FACTOR'''<br />
 
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==Overview==
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==The Crystal Structure of Human Supernatant Protein Factor==
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Supernatant protein factor (SPF) promotes the epoxidation of squalene, catalyzed by microsomes. Several studies suggest its in vivo role in the, cholesterol biosynthetic pathway by a yet unknown mechanism. SPF belongs, to a family of lipid binding proteins called CRAL_TRIO, which include, yeast phosphatidylinositol transfer protein Sec14 and tocopherol transfer, protein TTP. The crystal structure of human SPF at a resolution of 1.9 A, reveals a two domain topology. The N-terminal 275 residues form a, Sec14-like domain, while the C-terminal 115 residues consist of an, eight-stranded jelly-roll barrel similar to that found in many viral, protein structures. The ligand binding cavity has a peculiar, horseshoe-like shape. Contrary to the Sec14 crystal structure, the, lipid-exchange loop is in ... [[http://ispc.weizmann.ac.il/pmbin/getpm?12429094 (full description)]]
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<StructureSection load='1o6u' size='340' side='right'caption='[[1o6u]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1o6u]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O6U 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]] 2.05&#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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</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=1o6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6u OCA], [https://pdbe.org/1o6u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o6u RCSB], [https://www.ebi.ac.uk/pdbsum/1o6u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6u ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/S14L2_HUMAN S14L2_HUMAN] Carrier protein. Binds to some hydrophobic molecules and promotes their transfer between the different cellular sites. Binds with high affinity to alpha-tocopherol. Also binds with a weaker affinity to other tocopherols and to tocotrienols. May have a transcriptional activatory activity via its association with alpha-tocopherol. Probably recognizes and binds some squalene structure, suggesting that it may regulate cholesterol biosynthesis by increasing the transfer of squalene to a metabolic active pool in the cell.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o6/1o6u_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1o6u ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Supernatant protein factor (SPF) promotes the epoxidation of squalene catalyzed by microsomes. Several studies suggest its in vivo role in the cholesterol biosynthetic pathway by a yet unknown mechanism. SPF belongs to a family of lipid binding proteins called CRAL_TRIO, which include yeast phosphatidylinositol transfer protein Sec14 and tocopherol transfer protein TTP. The crystal structure of human SPF at a resolution of 1.9 A reveals a two domain topology. The N-terminal 275 residues form a Sec14-like domain, while the C-terminal 115 residues consist of an eight-stranded jelly-roll barrel similar to that found in many viral protein structures. The ligand binding cavity has a peculiar horseshoe-like shape. Contrary to the Sec14 crystal structure, the lipid-exchange loop is in a closed conformation, suggesting a mechanism for lipid exchange.
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==About this Structure==
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Crystal structure of the human supernatant protein factor.,Stocker A, Tomizaki T, Schulze-Briese C, Baumann U Structure. 2002 Nov;10(11):1533-40. PMID:12429094<ref>PMID:12429094</ref>
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1O6U is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with PLM as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O6U OCA]].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of the human supernatant protein factor., Stocker A, Tomizaki T, Schulze-Briese C, Baumann U, Structure. 2002 Nov;10(11):1533-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12429094 12429094]
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</div>
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<div class="pdbe-citations 1o6u" 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>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Schulze-Briese, C.]]
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[[Category: Schulze-Briese C]]
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[[Category: Stocker, A.]]
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[[Category: Stocker A]]
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[[Category: Tomizaki, T.]]
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[[Category: Tomizaki T]]
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[[Category: PLM]]
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[[Category: cral_trio]]
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[[Category: lipid binding]]
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[[Category: lipid transfer]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 16:55:38 2007''
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Current revision

The Crystal Structure of Human Supernatant Protein Factor

PDB ID 1o6u

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