 |
PDBsum entry 4c9c
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
The strawberry pathogenesis-Related 10 (pr-10) fra a proteins control flavonoid biosynthesis by binding to metabolic intermediates.
|
|
|
Authors
|
|
A.Casañal,
U.Zander,
C.Muñoz,
F.Dupeux,
I.Luque,
M.A.Botella,
W.Schwab,
V.Valpuesta,
J.A.Marquez.
|
|
|
Ref.
|
|
J Biol Chem, 2013,
288,
35322-35332.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
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.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Purification, Crystallization and preliminary X-Ray analysis of the strawberry allergens fra a 1e and fra a 3 in the presence of catechin.
|
|
|
Authors
|
|
A.Casañal,
U.Zander,
F.Dupeux,
V.Valpuesta,
J.A.Marquez.
|
|
|
Ref.
|
|
Acta Crystallogr Sect F Struct Biol Cryst Commun, 2013,
69,
510-514.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
