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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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Contents |
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* Residue conservation analysis
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DOI no:
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Protein Sci
7:2490-2498
(1998)
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PubMed id:
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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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M.H.Lerche,
F.M.Poulsen.
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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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Selected figure(s)
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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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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.P.Yang,
X.X.Ma,
Y.X.He,
W.F.Li,
Y.Kang,
R.Bao,
Y.Chen,
and
C.Z.Zhou
(2011).
Crystal structure of the 30K protein from the silkworm Bombyx mori reveals a new member of the β-trefoil superfamily.
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J Struct Biol,
175,
97.
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PDB code:
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D.Kümmel,
J.Walter,
M.Heck,
U.Heinemann,
and
M.Veit
(2010).
Characterization of the self-palmitoylation activity of the transport protein particle component Bet3.
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Cell Mol Life Sci,
67,
2653-2664.
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PDB code:
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K.Teilum,
J.G.Olsen,
and
B.B.Kragelund
(2009).
Functional aspects of protein flexibility.
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Cell Mol Life Sci,
66,
2231-2247.
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R.González-Rioja,
J.A.Asturias,
A.Martínez,
F.M.Goñi,
and
A.R.Viguera
(2009).
Par j 1 and Par j 2, the two major allergens in Parietaria judaica, bind preferentially to monoacylated negative lipids.
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FEBS J,
276,
1762-1775.
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F.Boutrot,
N.Chantret,
and
M.F.Gautier
(2008).
Genome-wide analysis of the rice and Arabidopsis non-specific lipid transfer protein (nsLtp) gene families and identification of wheat nsLtp genes by EST data mining.
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BMC Genomics,
9,
86.
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T.H.Yeats,
and
J.K.Rose
(2008).
The biochemistry and biology of extracellular plant lipid-transfer proteins (LTPs).
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Protein Sci,
17,
191-198.
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Y.T.Lai,
C.S.Cheng,
Y.N.Liu,
Y.J.Liu,
and
P.C.Lyu
(2008).
Effects of ligand binding on the dynamics of rice nonspecific lipid transfer protein 1: a model from molecular simulations.
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Proteins,
72,
1189-1198.
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J.Zídková,
P.Rehulka,
and
J.Chmelík
(2007).
Detection of hydrolysis of lipid post-translational modifications during gel-electrophoresis-based proteomic protocol.
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Proteomics,
7,
2507-2510.
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L.Zuidmeer,
and
R.van Ree
(2007).
Lipid transfer protein allergy: primary food allergy or pollen/food syndrome in some cases.
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Curr Opin Allergy Clin Immunol,
7,
269-273.
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K.Liu,
H.Jiang,
S.L.Moore,
C.B.Watkins,
and
M.M.Jahn
(2006).
Isolation and characterization of a lipid transfer protein expressed in ripening fruit of Capsicum chinense.
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Planta,
223,
672-683.
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P.Da Silva,
C.Landon,
R.Beltoise,
M.Ponchet,
and
F.Vovelle
(2006).
Accessibility of tobacco lipid transfer protein cavity revealed by 15N NMR relaxation studies and molecular dynamics simulations.
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Proteins,
64,
124-132.
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A.P.Turnbull,
D.Kümmel,
B.Prinz,
C.Holz,
J.Schultchen,
C.Lang,
F.H.Niesen,
K.P.Hofmann,
H.Delbrück,
J.Behlke,
E.C.Müller,
E.Jarosch,
T.Sommer,
and
U.Heinemann
(2005).
Structure of palmitoylated BET3: insights into TRAPP complex assembly and membrane localization.
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EMBO J,
24,
875-884.
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PDB code:
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F.Hoh,
J.L.Pons,
M.F.Gautier,
F.de Lamotte,
and
C.Dumas
(2005).
Structure of a liganded type 2 non-specific lipid-transfer protein from wheat and the molecular basis of lipid binding.
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Acta Crystallogr D Biol Crystallogr,
61,
397-406.
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PDB code:
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H.Breiteneder,
and
C.Mills
(2005).
Nonspecific lipid-transfer proteins in plant foods and pollens: an important allergen class.
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Curr Opin Allergy Clin Immunol,
5,
275-279.
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P.Da Silva,
C.Landon,
B.Industri,
A.Marais,
D.Marion,
M.Ponchet,
and
F.Vovelle
(2005).
Solution structure of a tobacco lipid transfer protein exhibiting new biophysical and biological features.
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Proteins,
59,
356-367.
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PDB code:
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S.C.Dias,
O.L.Franco,
C.P.Magalhães,
O.B.de Oliveira-Neto,
R.A.Laumann,
E.L.Figueira,
F.R.Melo,
and
M.F.Grossi-De-Sá
(2005).
Molecular cloning and expression of an alpha-amylase inhibitor from rye with potential for controlling insect pests.
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Protein J,
24,
113-123.
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H.C.Cheng,
P.T.Cheng,
P.Peng,
P.C.Lyu,
and
Y.J.Sun
(2004).
Lipid binding in rice nonspecific lipid transfer protein-1 complexes from Oryza sativa.
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Protein Sci,
13,
2304-2315.
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PDB codes:
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S.Y.Wang,
K.J.Zhou,
X.Y.Ye,
Z.B.Xu,
J.H.Wu,
and
P.F.Rao
(2004).
Crystallization and preliminary X-ray crystallographic analysis of a non-specific lipid-transfer protein with antipathogenic activity from Phaseolus mungo.
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Acta Crystallogr D Biol Crystallogr,
60,
2391-2393.
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D.K.Hincha
(2002).
Cryoprotectin: a plant lipid-transfer protein homologue that stabilizes membranes during freezing.
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Philos Trans R Soc Lond B Biol Sci,
357,
909-916.
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R.Lundheim
(2002).
Physiological and ecological significance of biological ice nucleators.
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Philos Trans R Soc Lond B Biol Sci,
357,
937-943.
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C.Landon,
P.Berthault,
F.Vovelle,
and
H.Desvaux
(2001).
Magnetization transfer from laser-polarized xenon to protons located in the hydrophobic cavity of the wheat nonspecific lipid transfer protein.
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Protein Sci,
10,
762-770.
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J.P.Douliez,
S.Jégou,
C.Pato,
D.Mollé,
V.Tran,
and
D.Marion
(2001).
Binding of two mono-acylated lipid monomers by the barley lipid transfer protein, LTP1, as viewed by fluorescence, isothermal titration calorimetry and molecular modelling.
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Eur J Biochem,
268,
384-388.
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J.P.Douliez,
T.Michon,
and
D.Marion
(2000).
Steady-state tyrosine fluorescence to study the lipid-binding properties of a wheat non-specific lipid-transfer protein (nsLTP1).
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Biochim Biophys Acta,
1467,
65-72.
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S.Tassin-Moindrot,
A.Caille,
J.P.Douliez,
D.Marion,
and
F.Vovelle
(2000).
The wide binding properties of a wheat nonspecific lipid transfer protein. Solution structure of a complex with prostaglandin B2.
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Eur J Biochem,
267,
1117-1124.
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PDB code:
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F.Guerbette,
M.Grosbois,
A.Jolliot-Croquin,
J.C.Kader,
and
A.Zachowski
(1999).
Comparison of lipid binding and transfer properties of two lipid transfer proteins from plants.
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Biochemistry,
38,
14131-14137.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
