4c9c
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4c9c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fragaria_x_ananassa Fragaria x ananassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C9C FirstGlance]. <br> | <table><tr><td colspan='2'>[[4c9c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fragaria_x_ananassa Fragaria x ananassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C9C FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.2Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4c9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9c OCA], [https://pdbe.org/4c9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c9c RCSB], [https://www.ebi.ac.uk/pdbsum/4c9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c9c 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=4c9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9c OCA], [https://pdbe.org/4c9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c9c RCSB], [https://www.ebi.ac.uk/pdbsum/4c9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c9c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/FRA1E_FRAAN FRA1E_FRAAN] Involved in the control of flavonoid biosynthesis in fruits, probably by binding directly to natural flavonoids (PubMed:19969523). Binds the natural flavonoid quercetin-3-O-glucuronide with affinities in the low micromolar range (PubMed:24133217).<ref>PMID:19969523</ref> <ref>PMID:24133217</ref> | |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pathogenesis-related 10 (PR-10) proteins are involved in many aspects of plant biology but their molecular function is still unclear. They are related by sequence and structural homology to mammalian lipid transport and plant abscisic acid receptor proteins, and are predicted to have cavities for ligand binding. Recently, three new members of the PR-10 family, the Fra a proteins, have been identified in strawberry, where they are required for the activity of the flavonoid biosynthesis pathway, which is essential for the development of color and flavor in fruits. Here we show that Fra a proteins bind natural flavonoids with different selectivity and affinities in the low muM range. The structural analysis of Fra a 1 E and a Fra a 3-catechin complex indicates that loops L3, L5 and L7, surrounding the ligand-binding cavity show significant flexibility in the apo forms, but close over the ligand in the Fra a 3-catechin complex. Our findings provide mechanistic insight on the function of Fra a proteins and suggest that PR-10 proteins, which are widespread in plants may play a role in the control of secondary metabolic pathways by binding to metabolic intermediates. | ||
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| + | The Strawberry Pathogenesis-Related 10 (PR-10) Fra a proteins control flavonoid biosynthesis by binding to metabolic intermediates.,Casanal A, Zander U, Munoz C, Dupeux F, Luque I, Botella MA, Schwab W, Valpuesta V, Marquez JA J Biol Chem. 2013 Oct 16. PMID:24133217<ref>PMID:24133217</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4c9c" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal Structure of the Strawberry Pathogenesis-Related 10 (PR-10) Fra a 1E protein (Form A)
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