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PDBsum entry 1be2
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Lipid transport
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PDB id
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1be2
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References listed in PDB file
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Key reference
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Title
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Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins.
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Authors
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M.H.Lerche,
F.M.Poulsen.
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Ref.
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Protein Sci, 1998,
7,
2490-2498.
[DOI no: ]
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PubMed id
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Abstract
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The structure of a nonspecific lipid transfer protein from barley (ns-LTPbarley)
in complex with palmitate has been determined by NMR spectroscopy. The structure
has been compared to the structure of ns-LTPbarley in the absence of palmitate,
to the structure of ns-LTPbarley in complex with palmitoyl coenzyme A, to the
structure of ns-LTPmaize in its free form, and to the maize protein complexed
with palmitate. Binding of palmitate only affects the structure of ns-LTPbarley
moderately in contrast to the binding of palmitoyl coenzyme A, which leads to a
considerable expansion of the protein. The modes of binding palmitate to the
maize and barley protein are different. Although in neither case there are major
conformational changes in the protein, the orientation of the palmitate in the
two proteins is exactly opposite.
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Figure 4.
Fig. 4. complex between ~ S-LT P~,~ ~ andpalmitate is shown as van
correspondinghydrophobicresiduesakecontact, the ontacts der Ns-LTPb=lv s shown ibbon structure. almitate is
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Figure 5.
Fig. 5. Differences in chemical shif fbackbone HN and H in liganded
and unligandednS-LTPbarley.determinedat pH .2. (A) Thedifferences in
HN; (B) thedifferences in H. Barsabovethecenteredzerolinerepresent
thecomparisonofthefreeform of ns-LTPbarley an thecomplexwith
PCoA.Barsbelowthecenteredzerolinerepresentsthecomparison of he
freeformofnS-LTPbarleyand the omplex with palmitateChanges in
chemicalshifts are primarily identified in heC-terminalregionofespe-
cially residueVa177-Ile8 1.
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The above figures are
reprinted
from an Open Access publication published by the Protein Society:
Protein Sci
(1998,
7,
2490-2498)
copyright 1998.
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Secondary reference #1
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Title
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Barley lipid-Transfer protein complexed with palmitoyl CoA: the structure reveals a hydrophobic binding site that can expand to fit both large and small lipid-Like ligands.
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Authors
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M.H.Lerche,
B.B.Kragelund,
L.M.Bech,
F.M.Poulsen.
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Ref.
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Structure, 1997,
5,
291-306.
[DOI no: ]
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PubMed id
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Figure 7.
Figure 7. A comparison of the minimized, lowest energy
structures of (a) liganded and (b) unliganded bLTP. The a
helices are coloured: red (H[A]), orange (H[B]), blue (H[C]) and
green (H[D]).
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The above figure is
reproduced from the cited reference
with permission from Cell Press
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Secondary reference #2
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Title
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Structure in solution of a four-Helix lipid binding protein.
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Authors
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B.Heinemann,
K.V.Andersen,
P.R.Nielsen,
L.M.Bech,
F.M.Poulsen.
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Ref.
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Protein Sci, 1996,
5,
13-23.
[DOI no: ]
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PubMed id
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Secondary reference #3
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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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