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PDBsum entry 2alg
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Lipid transport
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PDB id
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2alg
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References listed in PDB file
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Key reference
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Title
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Crystal structure of peach pru p 3, The prototypic member of the family of plant non-Specific lipid transfer protein pan-Allergens.
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Authors
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N.Pasquato,
R.Berni,
C.Folli,
S.Folloni,
M.Cianci,
S.Pantano,
J.R.Helliwell,
G.Zanotti.
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Ref.
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J Mol Biol, 2006,
356,
684-694.
[DOI no: ]
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PubMed id
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Abstract
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This study describes the three-dimensional crystal structure of a non-specific
lipid transport protein (ns-LTP) from Rosaceae. Whilst ns-LTPs from species
other than Rosaceae, such as nuts, cereals, grape, oranges and vegetables are
also responsible for plant food allergies, this is less frequent compared with
ns-LTPs from Rosaceae in the Mediterranean area. In this heterologously
expressed peach Pru p3, a ligand is present inside the central cavity of the
protein, presumably a fatty acid that was present or produced in the culture
medium of the expression organism Escherichia coli. Moreover, the two molecules
of ns-LTP present in the asymmetric unit bind this ligand in a different way,
suggesting a significant degree of plasticity for the peach ns-LTP binding
cavity, despite the presence of four disulphide bridges. Two molecules are
present in the asymmetric unit: molecule A is a fully liganded protein, while
molecule B apparently represents a partially liganded state. Also, molecular
dynamics simulation, along with other evidence, suggests that these two
molecular conformations represent different states in solution. Comparison of
the 3D models of different ns-LTPs justifies the evidence of a high degree of
conservation of the putative IgE binding epitopes among proteins of the Rosaceae
family and the presence of significant amino acid replacements in correspondence
of the same regions in ns-LTPs of botanical species unrelated to Rosaceae.
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Figure 1.
Figure 1. (a) Stereo view of the C^a chain trace of
molecule A of peach ns-LTP. The two hypothetical ligands (or the
two orientations of the ligand) inside the cavity are shown
(ball-and-stick model). The disulphide bridges are denoted by
broken lines. (b) Same as (a), for molecule B.
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Figure 2.
Figure 2. (a) Superposition of the ligands of wheat ns-LTP
A molecule (1BWO PDB code) on the ligand of peach ns-LTP A and B
molecules. The image shows the following elements: transparent
van der Waals surface of peach ns-LTP, molecule A; stick view of
the peach protein A (red) and B (green) ligands and stick
representation of the two wheat ns-LTP
lyso-palmytoyl-phosphatidylcholine ligands (yellow). (b)
Superposition of ribbon models of molecules A (blue) and B
(green). Ligands of molecule A are shown as CPK spheres. The
Tyr79 side-chain of molecule B partially occupies the position
of one of molecule A ligands (see the text for details).
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2006,
356,
684-694)
copyright 2006.
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Secondary reference #1
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Title
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High-Resolution crystal structure of the non-Specific lipid-Transfer protein from maize seedlings.
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Authors
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D.H.Shin,
J.Y.Lee,
K.Y.Hwang,
K.K.Kim,
S.W.Suh.
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Ref.
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Structure, 1995,
3,
189-199.
[DOI no: ]
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PubMed id
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Figure 3.
Figure 3. Comparison of disulfide bridge patterns and secondary
structures of maize ns-LTP (a) and hydrophobic protein from
soybean (b). H, α-helix; G, 3[10]-helix; S, β-strand; L,
loop. Figure 3. Comparison of disulfide bridge patterns and
secondary structures of maize ns-LTP (a) and hydrophobic protein
from soybean (b). H, α-helix; G, 3[10]-helix; S, β-strand; L,
loop.
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Figure 4.
Figure 4. Stereo diagram showing the amino acid distribution in
uncomplexed maize ns-LTP. Basic residues (Arg, Lys) are colored
cyan; acidic residues (Asp), red; neutral polar residues (Asn,
Gln, Gly, Ser, Thr), orange; Tyr, white; hydrophobic residues
(Ala, Ile, Leu, Pro, Val), pink; Cys, yellow. Figure 4.
Stereo diagram showing the amino acid distribution in
uncomplexed maize ns-LTP. Basic residues (Arg, Lys) are colored
cyan; acidic residues (Asp), red; neutral polar residues (Asn,
Gln, Gly, Ser, Thr), orange; Tyr, white; hydrophobic residues
(Ala, Ile, Leu, Pro, Val), pink; Cys, yellow.
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The above figures are
reproduced from the cited reference
with permission from Cell Press
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