4lej
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4lej]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pinus_koraiensis Pinus koraiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LEJ FirstGlance]. <br> | <table><tr><td colspan='2'>[[4lej]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pinus_koraiensis Pinus koraiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LEJ FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.402Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4lej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lej OCA], [https://pdbe.org/4lej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lej RCSB], [https://www.ebi.ac.uk/pdbsum/4lej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lej 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=4lej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lej OCA], [https://pdbe.org/4lej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lej RCSB], [https://www.ebi.ac.uk/pdbsum/4lej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lej ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/VCL_PINKO VCL_PINKO] Seed storage protein.<ref>PMID:18084088</ref> <ref>PMID:18690685</ref> | [https://www.uniprot.org/uniprot/VCL_PINKO VCL_PINKO] Seed storage protein.<ref>PMID:18084088</ref> <ref>PMID:18690685</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The prevalence of food allergy has increased in recent years, and Korean pine vicilin is a potential food allergen. We have previously reported the crystallization of Korean pine vicilin purified from raw pine nut. Here we report the isolation of vicilin mRNA and the crystal structure of Korean pine vicilin at 2.40 A resolution. The overall structure of pine nut vicilin is similar to the structures of other 7S seed storage proteins and consists of an N-terminal domain and a C-terminal domain. Each assumes a cupin fold, and they are symmetrically related about a pseudodyad axis. Three vicilin molecules form a doughnut-shaped trimer through head-to-tail association. Structure characterization of Korean pine nut vicilin unexpectedly showed that, in its native trimeric state, the vicilin has three copper ligands. Sequence alignments suggested that the copper-coordinating residues were conserved in winter squash, sesame, tomato, and several tree nuts, while they were not conserved in a number of legumes, including peanut and soybean. Additional studies are needed to assess whether the copper-coordinating property of vicilins has a biological function in the relevant plants. The nutritional value of this copper-coordinating protein in tree nuts and other edible seeds may be worth further investigations. | ||
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| - | Crystal Structure of Korean Pine ( Pinus koraiensis ) 7S Seed Storage Protein with Copper Ligands.,Jin T, Wang Y, Chen YW, Fu TJ, Kothary MH, McHugh TH, Zhang Y J Agric Food Chem. 2013 Dec 23. PMID:24328105<ref>PMID:24328105</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4lej" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal Structure of the Korean pine (Pinus koraiensis) vicilin
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