4C94
Crystal Structure of the Strawberry Pathogenesis-Related 10 (PR-10) Fra a 3 protein in complex with Catechin
Summary for 4C94
Entry DOI | 10.2210/pdb4c94/pdb |
Descriptor | FRA A 3 ALLERGEN, (2R,3S)-2-(3,4-dihydroxyphenyl)-3,4-dihydro-2H-chromene-3,5,7-triol (3 entities in total) |
Functional Keywords | allergen, pyr/pyl/rcar, bet v 1, flavonoids |
Biological source | FRAGARIA X ANANASSA (STRAWBERRY) |
Total number of polymer chains | 5 |
Total formula weight | 89826.58 |
Authors | Casanal, A.,Zander, U.,Valpuesta, V.,Marquez, J.A. (deposition date: 2013-10-02, release date: 2013-10-16, Last modification date: 2023-12-20) |
Primary citation | Casanal, A.,Zander, U.,Munoz, C.,Dupeux, F.,Luque, I.,Botella, M.A.,Schwab, W.,Valpuesta, V.,Marquez, J.A. The Strawberry Pathogenesis-Related 10 (Pr-10) Fra a Proteins Control Flavonoid Biosynthesis by Binding to Metabolic Intermediates. J.Biol.Chem., 288:35322-, 2013 Cited by PubMed Abstract: 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 μm 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. PubMed: 24133217DOI: 10.1074/JBC.M113.501528 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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