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PDBsum entry 1fk3
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Lipid transport
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PDB id
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1fk3
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structural basis of non-Specific lipid binding in maize lipid-Transfer protein complexes revealed by high-Resolution x-Ray crystallography.
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Authors
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G.W.Han,
J.Y.Lee,
H.K.Song,
C.Chang,
K.Min,
J.Moon,
D.H.Shin,
M.L.Kopka,
M.R.Sawaya,
H.S.Yuan,
T.D.Kim,
J.Choe,
D.Lim,
H.J.Moon,
S.W.Suh.
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Ref.
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J Mol Biol, 2001,
308,
263-278.
[DOI no: ]
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PubMed id
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Abstract
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Non-specific lipid-transfer proteins (nsLTPs) are involved in the movement of
phospholipids, glycolipids, fatty acids, and steroids between membranes. Several
structures of plant nsLTPs have been determined both by X-ray crystallography
and nuclear magnetic resonance. However, the detailed structural basis of the
non-specific binding of hydrophobic ligands by nsLTPs is still poorly
understood. In order to gain a better understanding of the structural basis of
the non-specific binding of hydrophobic ligands by nsLTPs and to investigate the
plasticity of the fatty acid binding cavity in nsLTPs, seven high-resolution
(between 1.3 A and 1.9 A) crystal structures have been determined. These depict
the nsLTP from maize seedlings in complex with an array of fatty acids.A
detailed comparison of the structures of maize nsLTP in complex with various
ligands reveals a new binding mode in an nsLTP-oleate complex which has not been
seen before. Furthermore, in the caprate complex, the ligand binds to the
protein cavity in two orientations with equal occupancy. The volume of the
hydrophobic cavity in the nsLTP from maize shows some variation depending on the
size of the bound ligands.The structural plasticity of the ligand binding cavity
and the predominant involvement of non-specific van der Waals interactions with
the hydrophobic tail of the ligands provide a structural explanation for the
non-specificity of maize nsLTP. The hydrophobic cavity accommodates various
ligands from C10 to C18. The C18:1 ricinoleate with its hydroxyl group hydrogen
bonding to Ala68 possibly mimics cutin monomer binding which is of biological
importance. Some of the myristate binding sites in human serum albumin resemble
the maize nsLTP, implying the importance of a helical bundle in accommodating
the non-specific binding of fatty acids.
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Figure 1.
Figure 1. (a) Stereo ribbon diagram of maize non-specific
lipid-transfer protein complexed with oleate. The Figures were
drawn with the MOLSCRIPT program.41 (b) Superposition of the
backbone trace of eight nsLTP complexes. (c) Bound fatty acids
showing structural comparisons between complexes. Colors used in
(b) and (c): nsLTP:caprate (purple), nsLTP:laurate (red),
nsLTP:myristate (dark red), nsLTP:palmitoleate (green),
nsLTP-stearate (blue), nsLTP:oleate (dark green),
nsLTP-linoleneate (yellow), and nsLTP-ricinoleate (dark blue).
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Figure 6.
Figure 6. Comparisons of nsLTP:myristate with human serum
albumin (HSA) in complex with myristate moieties. Insight II
v97.5 (Molecular Simulations, Inc.) was used for the display.
The three domains of HSA bind five myristate moieties; four are
shown here, myr1, myr3, myr4, and myr5.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2001,
308,
263-278)
copyright 2001.
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