Purification, crystallization and preliminary X‐ray analysis of the strawberry allergens Fra a 1E and Fra a 3 in the presence of catechin. Issue 5 (22nd May 2013)

• Record Type: Journal Article
• Authors: Casañal, Ana; Zander, Ulrich; Dupeux, Florine; Valpuesta, Victoriano; Marquez, Jose A.
• Is Part Of: Acta crystallographica. Volume 69:Issue 5(2013:May)
• Page Start: 510
• Page End: 514
• Publication Date: 2013-05-22
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113006945
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The strawberry Fra a proteins belong to the pathogenesis‐related PR‐10 protein family and share a common fold with the Bet v 1 major pollen allergen and the START/PYR/PYL proteins, which are characterized by the presence of a central cavity and are often involved in the binding of a variety of natural compounds. The Fra a proteins play a key role in the control of flavonoid biosynthesis in strawberries and are essential for pigment formation in fruits. In order to understand Fra a protein function, full‐length <italic>Fra a 1E</italic> and <italic>Fra a 3</italic> cDNAs were cloned and expressed in <italic>Escherichia coli</italic>, and the proteins were purified to homogeneity using metal‐affinity chromatography. Diffraction‐quality crystals of Fra a 1E and of Fra a 3 in the presence of (+)‐catechin were obtained by the sitting‐drop vapour‐diffusion method. X‐ray diffraction data from single crystals of Fra a 1E and Fra a 3 were processed to 2.2 and 3.0 Å resolution in space groups <italic>P</italic>2₁2₁2₁ and <italic>P</italic>222₁, with unit‐cell parameters <italic>a</italic> = 70.02, <italic>b</italic> = 74.42, <italic>c</italic> = 84.04 Å and <italic>a</italic> = 137.91, <italic>b</italic> = 206.61, <italic>c</italic> = 174.7 Å for Fra a 1E and Fra a 3, respectively.</p> </abstract>