4c94 | pdb_00004c94
Crystal Structure of the Strawberry Pathogenesis-Related 10 (PR-10) Fra a 3 protein in complex with Catechin
Structural highlights
FunctionFRA13_FRAAN Involved in the control of flavonoid biosynthesis in fruits, probably by binding directly to natural flavonoids (PubMed:19969523). Binds the natural flavonoid catechin with affinities in the low micromolar range (PubMed:24133217).[1] [2] Publication Abstract from PubMedPathogenesis-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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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