PDBsum entry 4c9c

Allergen

PDB id: 4c9c

Contents

Protein chains

158 a.a.

Ligands

SO4 ×2

GOL ×2

Waters ×157

PDB id:

4c9c

Name:

Allergen

Title:

Crystal structure of the strawberry pathogenesis-related 10 (pr-10) fra a 1e protein (form a)

Structure:

Major strawberry allergen fra a 1-e. Chain: a, b. Synonym: fra a 1e. Engineered: yes

Source:

Fragaria x ananassa. Strawberry. Organism_taxid: 3747. Expressed in: escherichia coli. Expression_system_taxid: 511693.

Resolution:

2.20Å R-factor: 0.208 R-free: 0.250

Authors:

A.Casanal,U.Zander,V.Valpuesta,J.A.Marquez

Key ref:

A.Casañal et al. (2013). The strawberry pathogenesis-related 10 (PR-10) Fra a proteins control flavonoid biosynthesis by binding to metabolic intermediates. J Biol Chem, 288, 35322-35332. PubMed id: 24133217 DOI: 10.1074/jbc.M113.501528

Date:

02-Oct-13 Release date: 16-Oct-13

Protein chains

Q256S2  (FRA1E_FRAAN) -  Major strawberry allergen Fra a 1-E from Fragaria ananassa

Seq: 160 a.a.

Struc: 158 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1074/jbc.M113.501528

J Biol Chem 288:35322-35332 (2013)

PubMed id: 24133217

The strawberry pathogenesis-related 10 (PR-10) Fra a proteins control flavonoid biosynthesis by binding to metabolic intermediates.

A.Casañal, U.Zander, C.Muñoz, F.Dupeux, I.Luque, M.A.Botella, W.Schwab, V.Valpuesta, J.A.Marquez.

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.