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* Residue conservation analysis
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PDB id:
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Lectin
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Title:
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Three-dimensional structures of complexes of lathyrus ochrus isolectin i with glucose and mannose: fine specificity of the monosaccharide- binding site
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Structure:
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Legume isolectin i (alpha chain). Chain: a, c, e, g. Engineered: yes. Legume isolectin i (beta chain). Chain: b, d, f, h. Engineered: yes
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Source:
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Lathyrus ochrus. Yellow-flowered pea. Organism_taxid: 3858. Organ: seed. Organ: seed
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Biol. unit:
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Tetramer (from
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Resolution:
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Authors:
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Y.Bourne,C.Cambillau
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Key ref:
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Y.Bourne
et al.
(1990).
Three-dimensional structures of complexes of Lathyrus ochrus isolectin I with glucose and mannose: fine specificity of the monosaccharide-binding site.
Proteins,
8,
365-376.
PubMed id:
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Date:
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27-Jan-93
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Release date:
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30-Apr-94
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PROCHECK
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Headers
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References
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P04122
(LECB_LATOC) -
Lectin beta-1 and beta-2 chains from Lathyrus ochrus
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Seq: Struc:
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181 a.a.
180 a.a.*
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Enzyme class:
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Chains A, B, C, D, E, F, G, H:
E.C.?
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Proteins
8:365-376
(1990)
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PubMed id:
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Three-dimensional structures of complexes of Lathyrus ochrus isolectin I with glucose and mannose: fine specificity of the monosaccharide-binding site.
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Y.Bourne,
A.Roussel,
M.Frey,
P.Rougé,
J.C.Fontecilla-Camps,
C.Cambillau.
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ABSTRACT
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The structure of the methyl-alpha-D-mannopyranoside-LOL I complex has been
solved by the molecular replacement method using the refined saccharide-free LOL
I coordinates as starting model. The methyl-alpha-D-mannopyranoside-LOL I
complex was refined by simulated annealing using the program X-PLOR. The final
R-factor value is 0.182 [Fo greater than 1 sigma(Fo)]. The isostructural
methyl-alpha-D-glucopyranoside-LOL I complex was refined by X-Ray coupled energy
minimization using the methyl-alpha-D-mannopyranoside-LOL I structure as a
starting model to an R factor of 0.179 (all data). In both crystal forms, each
dimer binds two molecules of sugar in pockets found near the calcium ions. The
two saccharide moieties, which are in the C1 chair conformation, establish the
same hydrogen bond pattern with the lectin. However, the van der Waals contacts
are different between the O2, C2, C6, and O6 atoms of the two molecules and the
backbone atoms of residues 208-211. Mannose, due to its axial C2 conformation,
encloses the backbone atoms of the protein in a clamplike way. Van der Waals
energy calculations suggest that this better complementarity of the mannoside
molecule with the lectin could explain its higher affinity for isolectin I.
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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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B.A.Rocha,
P.Delatorre,
T.M.Oliveira,
R.G.Benevides,
A.F.Pires,
A.A.Sousa,
L.A.Souza,
A.M.Assreuy,
H.Debray,
W.F.de Azevedo,
A.H.Sampaio,
and
B.S.Cavada
(2011).
Structural basis for both pro- and anti-inflammatory response induced by mannose-specific legume lectin from Cymbosema roseum.
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Biochimie,
93,
806-816.
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PDB code:
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E.J.Cocinero,
E.C.Stanca-Kaposta,
E.M.Scanlan,
D.P.Gamblin,
B.G.Davis,
and
J.P.Simons
(2008).
Conformational choice and selectivity in singly and multiply hydrated monosaccharides in the gas phase.
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Chemistry,
14,
8947-8955.
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G.Sciara,
S.Blangy,
M.Siponen,
S.Mc Grath,
D.van Sinderen,
M.Tegoni,
C.Cambillau,
and
V.Campanacci
(2008).
A topological model of the baseplate of lactococcal phage tuc2009.
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J Biol Chem,
283,
2716-2723.
|
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|
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P.K.Qasba,
B.Ramakrishnan,
and
E.Boeggeman
(2008).
Structure and function of beta -1,4-galactosyltransferase.
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Curr Drug Targets,
9,
292-309.
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D.M.Tremblay,
M.Tegoni,
S.Spinelli,
V.Campanacci,
S.Blangy,
C.Huyghe,
A.Desmyter,
S.Labrie,
S.Moineau,
and
C.Cambillau
(2006).
Receptor-binding protein of Lactococcus lactis phages: identification and characterization of the saccharide receptor-binding site.
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J Bacteriol,
188,
2400-2410.
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PDB code:
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P.K.Qasba,
B.Ramakrishnan,
and
E.Boeggeman
(2006).
Mutant glycosyltransferases assist in the development of a targeted drug delivery system and contrast agents for MRI.
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AAPS J,
8,
E190-E195.
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S.Ricagno,
V.Campanacci,
S.Blangy,
S.Spinelli,
D.Tremblay,
S.Moineau,
M.Tegoni,
and
C.Cambillau
(2006).
Crystal structure of the receptor-binding protein head domain from Lactococcus lactis phage bIL170.
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J Virol,
80,
9331-9335.
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PDB code:
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S.Spinelli,
A.Desmyter,
C.T.Verrips,
H.J.de Haard,
S.Moineau,
and
C.Cambillau
(2006).
Lactococcal bacteriophage p2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses.
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Nat Struct Mol Biol,
13,
85-89.
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PDB codes:
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T.Satoh,
K.Sato,
A.Kanoh,
K.Yamashita,
Y.Yamada,
N.Igarashi,
R.Kato,
A.Nakano,
and
S.Wakatsuki
(2006).
Structures of the carbohydrate recognition domain of Ca2+-independent cargo receptors Emp46p and Emp47p.
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J Biol Chem,
281,
10410-10419.
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PDB codes:
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R.Loris,
A.Imberty,
S.Beeckmans,
E.Van Driessche,
J.S.Read,
J.Bouckaert,
H.De Greve,
L.Buts,
and
L.Wyns
(2003).
Crystal structure of Pterocarpus angolensis lectin in complex with glucose, sucrose, and turanose.
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J Biol Chem,
278,
16297-16303.
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PDB codes:
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L.J.Olson,
J.Zhang,
N.M.Dahms,
and
J.J.Kim
(2002).
Twists and turns of the cation-dependent mannose 6-phosphate receptor. Ligand-bound versus ligand-free receptor.
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J Biol Chem,
277,
10156-10161.
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PDB code:
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L.M.Velloso,
K.Svensson,
G.Schneider,
R.F.Pettersson,
and
Y.Lindqvist
(2002).
Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum.
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J Biol Chem,
277,
15979-15984.
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PDB code:
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A.Rabijns,
C.Verboven,
P.Rougé,
A.Barre,
E.J.Van Damme,
W.J.Peumans,
and
C.J.De Ranter
(2001).
Structure of a legume lectin from the bark of Robinia pseudoacacia and its complex with N-acetylgalactosamine.
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Proteins,
44,
470-478.
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PDB codes:
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R.Ravishankar,
C.J.Thomas,
K.Suguna,
A.Surolia,
and
M.Vijayan
(2001).
Crystal structures of the peanut lectin-lactose complex at acidic pH: retention of unusual quaternary structure, empty and carbohydrate bound combining sites, molecular mimicry and crystal packing directed by interactions at the combining site.
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Proteins,
43,
260-270.
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PDB codes:
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E.García-Hernández,
and
A.Hernández-Arana
(1999).
Structural bases of lectin-carbohydrate affinities: comparison with protein-folding energetics.
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Protein Sci,
8,
1075-1086.
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N.Manoj,
V.R.Srinivas,
and
K.Suguna
(1999).
Structure of basic winged-bean lectin and a comparison with its saccharide-bound form.
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Acta Crystallogr D Biol Crystallogr,
55,
794-800.
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PDB code:
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Y.Bourne,
V.Zamboni,
A.Barre,
W.J.Peumans,
E.J.Van Damme,
and
P.Rougé
(1999).
Helianthus tuberosus lectin reveals a widespread scaffold for mannose-binding lectins.
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Structure,
7,
1473-1482.
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PDB codes:
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L.Mourey,
J.D.Pédelacq,
C.Birck,
C.Fabre,
P.Rougé,
and
J.P.Samama
(1998).
Crystal structure of the arcelin-1 dimer from Phaseolus vulgaris at 1.9-A resolution.
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J Biol Chem,
273,
12914-12922.
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PDB code:
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W.Cheng,
E.Bullitt,
L.Bhattacharyya,
C.F.Brewer,
and
L.Makowski
(1998).
Electron microscopy and x-ray diffraction studies of Lotus tetragonolobus A isolectin cross-linked with a divalent Lewisx oligosaccharide, an oncofetal antigen.
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J Biol Chem,
273,
35016-35022.
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K.Drickamer
(1997).
Making a fitting choice: common aspects of sugar-binding sites in plant and animal lectins.
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Structure,
5,
465-468.
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C.Itin,
A.C.Roche,
M.Monsigny,
and
H.P.Hauri
(1996).
ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.
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Mol Biol Cell,
7,
483-493.
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J.H.Naismith,
and
R.A.Field
(1996).
Structural basis of trimannoside recognition by concanavalin A.
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J Biol Chem,
271,
972-976.
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PDB code:
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R.Adar,
and
N.Sharon
(1996).
Mutational studies of the amino acid residues in the combining site of Erythrina corallodendron lectin.
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Eur J Biochem,
239,
668-674.
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T.W.Hamelryck,
F.Poortmans,
A.Goossens,
G.Angenon,
M.Van Montagu,
L.Wyns,
and
R.Loris
(1996).
Crystal structure of arcelin-5, a lectin-like defense protein from Phaseolus vulgaris.
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J Biol Chem,
271,
32796-32802.
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PDB code:
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Y.Konami,
K.Yamamoto,
T.Osawa,
and
T.Irimura
(1995).
A putative carbohydrate-binding domain of the lactose-binding Cytisus sessilifolius anti-H(O) lectin has a similar amino acid sequence to that of the L-fucose-binding Ulex europaeus anti-H(O) lectin.
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Glycoconj J,
12,
128-134.
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A.Imberty,
F.Casset,
C.V.Gegg,
M.E.Etzler,
and
S.Pérez
(1994).
Molecular modelling of the Dolichos biflorus seed lectin and its specific interactions with carbohydrates: alpha-D-N-acetyl-galactosamine, Forssman disaccharide and blood group A trisaccharide.
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Glycoconj J,
11,
400-413.
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R.Loris,
D.Van Overberge,
M.H.Dao-Thi,
F.Poortmans,
N.Maene,
and
L.Wyns
(1994).
Structural analysis of two crystal forms of lentil lectin at 1.8 A resolution.
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Proteins,
20,
330-346.
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PDB codes:
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R.Loris,
F.Casset,
J.Bouckaert,
J.Pletinckx,
M.H.Dao-Thi,
F.Poortmans,
A.Imberty,
S.Perez,
and
L.Wyns
(1994).
The monosaccharide binding site of lentil lectin: an X-ray and molecular modelling study.
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Glycoconj J,
11,
507-517.
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PDB code:
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Y.Bourne,
J.Mazurier,
D.Legrand,
P.Rougé,
J.Montreuil,
G.Spik,
and
C.Cambillau
(1994).
Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety.
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Structure,
2,
209-219.
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PDB codes:
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N.Sharon
(1993).
Lectin-carbohydrate complexes of plants and animals: an atomic view.
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Trends Biochem Sci,
18,
221-226.
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A.Ayouba,
H.Debray,
and
P.Rougé
(1992).
Fine sugar specificity of the Butea frondosa seed lectin.
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Glycoconj J,
9,
141-147.
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J.K.Scott,
D.Loganathan,
R.B.Easley,
X.Gong,
and
I.J.Goldstein
(1992).
A family of concanavalin A-binding peptides from a hexapeptide epitope library.
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Proc Natl Acad Sci U S A,
89,
5398-5402.
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A.Ayouba,
C.Chatelain,
and
P.Rougé
(1991).
Legume lectins interact with muramic acid and N-acetylmuramic acid.
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FEBS Lett,
289,
102-104.
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J.A.Tainer,
V.A.Roberts,
and
E.D.Getzoff
(1991).
Metal-binding sites in proteins.
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Curr Opin Biotechnol,
2,
582-591.
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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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