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PDBsum entry 1j4t
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Plant protein
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PDB id
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1j4t
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Contents |
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* Residue conservation analysis
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PDB id:
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Plant protein
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Title:
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Structure of artocarpin: a lectin with mannose specificity (form 2)
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Structure:
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Artocarpin. Chain: a, b, c, d, e, f, g, h
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Source:
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Artocarpus integer. Organism_taxid: 3490. Other_details: seeds
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Biol. unit:
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Tetramer (from
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Resolution:
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2.40Å
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R-factor:
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0.191
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R-free:
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0.258
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Authors:
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J.V.Pratap,A.A.Jeyaprakash,P.G.Rani,K.Sekar,A.Surolia,M.Vijayan
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Key ref:
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J.V.Pratap
et al.
(2002).
Crystal structures of artocarpin, a Moraceae lectin with mannose specificity, and its complex with methyl-alpha-D-mannose: implications to the generation of carbohydrate specificity.
J Mol Biol,
317,
237-247.
PubMed id:
DOI:
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Date:
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30-Oct-01
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Release date:
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27-Mar-02
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PROCHECK
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Headers
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References
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Q7M1T4
(Q7M1T4_ARTIN) -
Mannose-specific lectin KM+ from Artocarpus integer
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Seq: Struc:
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149 a.a.
149 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 8 residue positions (black
crosses)
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DOI no:
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J Mol Biol
317:237-247
(2002)
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PubMed id:
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Crystal structures of artocarpin, a Moraceae lectin with mannose specificity, and its complex with methyl-alpha-D-mannose: implications to the generation of carbohydrate specificity.
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J.V.Pratap,
A.A.Jeyaprakash,
P.G.Rani,
K.Sekar,
A.Surolia,
M.Vijayan.
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ABSTRACT
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The seeds of jack fruit (Artocarpus integrifolia) contain two tetrameric
lectins, jacalin and artocarpin. Jacalin was the first lectin found to exhibit
the beta-prism I fold, which is characteristic of the Moraceae plant lectin
family. Jacalin contains two polypeptide chains produced by a post-translational
proteolysis which has been shown to be crucial for generating its specificity
for galactose. Artocarpin is a single chain protein with considerable sequence
similarity with jacalin. It, however, exhibits many properties different from
those of jacalin. In particular, it is specific to mannose. The structures of
two crystal forms, form I and form II, of the native lectin have been determined
at 2.4 and 2.5 A resolution, respectively. The structure of the lectin complexed
with methyl-alpha-mannose, has also been determined at 2.9 A resolution. The
structure is similar to jacalin, although differences exist in details. The
crystal structures and detailed modelling studies indicate that the following
differences between the carbohydrate binding sites of artocarpin and jacalin are
responsible for the difference in the specificities of the two lectins. Firstly,
artocarpin does not contain, unlike jacalin, an N terminus generated by
post-translational proteolysis. Secondly, there is no aromatic residue in the
binding site of artocarpin whereas there are four in that of jacalin. A
comparison with similar lectins of known structures or sequences, suggests that,
in general, stacking interactions with aromatic residues are important for the
binding of galactose while such interactions are usually absent in the
carbohydrate binding sites of mannose-specific lectins with the beta-prism I
fold.
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Selected figure(s)
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Figure 1.
Figure 1. Structure of artocarpin. (a) Schematic
representation showing hydrogen bonds. (b) The subunit with the
three Greek keys coloured differently. (c) Quaternary structure
with the four subunits coloured differently. Figures 1(b) 4 were
prepared using BOBSCRIPT. [44]
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Figure 3.
Figure 3. (a) Stereo view of the sugar molecule in the A
subunit with the 2|F[o]| -|F[c]| map contoured at 1s and (b)
hydrogen bonds observed between the protein and sugar.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2002,
317,
237-247)
copyright 2002.
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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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A.Sharma,
and
M.Vijayan
(2011).
Influence of glycosidic linkage on the nature of carbohydrate binding in beta-prism I fold lectins: an X-ray and molecular dynamics investigation on banana lectin-carbohydrate complexes.
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Glycobiology,
21,
23-33.
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PDB codes:
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G.Gupta,
S.Vishveshwara,
and
A.Surolia
(2009).
Stability of dimeric interface in banana lectin: Insight from molecular dynamics simulations.
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IUBMB Life,
61,
252-260.
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G.Gupta,
S.Sinha,
and
A.Surolia
(2008).
Unfolding energetics and stability of banana lectin.
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Proteins,
72,
754-760.
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S.Nakamura-Tsuruta,
N.Uchiyama,
W.J.Peumans,
E.J.Van Damme,
K.Totani,
Y.Ito,
and
J.Hirabayashi
(2008).
Analysis of the sugar-binding specificity of mannose-binding-type Jacalin-related lectins by frontal affinity chromatography--an approach to functional classification.
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FEBS J,
275,
1227-1239.
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A.Sharma,
D.Chandran,
D.D.Singh,
and
M.Vijayan
(2007).
Multiplicity of carbohydrate-binding sites in beta-prism fold lectins: occurrence and possible evolutionary implications.
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J Biosci,
32,
1089-1110.
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C.R.Pigott,
and
D.J.Ellar
(2007).
Role of receptors in Bacillus thuringiensis crystal toxin activity.
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Microbiol Mol Biol Rev,
71,
255-281.
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F.S.Kittur,
M.Lalgondar,
H.Y.Yu,
D.R.Bevan,
and
A.Esen
(2007).
Maize beta-glucosidase-aggregating factor is a polyspecific jacalin-related chimeric lectin, and its lectin domain is responsible for beta-glucosidase aggregation.
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J Biol Chem,
282,
7299-7311.
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M.Vijayan
(2007).
Peanut lectin crystallography and macromolecular structural studies in India.
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J Biosci,
32,
1059-1066.
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K.N.Rao,
D.Kumaran,
J.Seetharaman,
J.B.Bonanno,
S.K.Burley,
and
S.Swaminathan
(2006).
Crystal structure of trehalose-6-phosphate phosphatase-related protein: biochemical and biological implications.
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Protein Sci,
15,
1735-1744.
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PDB code:
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K.Sumathi,
P.Ananthalakshmi,
M.N.Roshan,
and
K.Sekar
(2006).
3dSS: 3D structural superposition.
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Nucleic Acids Res,
34,
W128-W132.
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S.S.Komath,
M.Kavitha,
and
M.J.Swamy
(2006).
Beyond carbohydrate binding: new directions in plant lectin research.
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Org Biomol Chem,
4,
973-988.
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T.Haraguchi,
K.Nomura,
and
F.Yagi
(2006).
Cloning and expression of a mannose-binding jacalin-related lectin from leaves of Japanese cycad (Cycas revoluta Thunb.).
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Biosci Biotechnol Biochem,
70,
2222-2229.
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A.Rabijns,
A.Barre,
E.J.Van Damme,
W.J.Peumans,
C.J.De Ranter,
and
P.Rougé
(2005).
Structural analysis of the jacalin-related lectin MornigaM from the black mulberry (Morus nigra) in complex with mannose.
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FEBS J,
272,
3725-3732.
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PDB codes:
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F.Gallego del Sol,
J.Gómez,
S.Hoos,
C.S.Nagano,
B.S.Cavada,
P.England,
and
J.J.Calvete
(2005).
Energetics of 5-bromo-4-chloro-3-indolyl-alpha-D-mannose binding to the Parkia platycephala seed lectin and its use for MAD phasing.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
61,
326-331.
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S.Nakamura,
F.Yagi,
K.Totani,
Y.Ito,
and
J.Hirabayashi
(2005).
Comparative analysis of carbohydrate-binding properties of two tandem repeat-type Jacalin-related lectins, Castanea crenata agglutinin and Cycas revoluta leaf lectin.
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FEBS J,
272,
2784-2799.
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D.D.Singh,
K.Saikrishnan,
P.Kumar,
Z.Dauter,
K.Sekar,
A.Surolia,
and
M.Vijayan
(2004).
Purification, crystallization and preliminary X-ray structure analysis of the banana lectin from Musa paradisiaca.
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Acta Crystallogr D Biol Crystallogr,
60,
2104-2106.
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K.N.Rao,
C.G.Suresh,
U.V.Katre,
S.M.Gaikwad,
and
M.I.Khan
(2004).
Two orthorhombic crystal structures of a galactose-specific lectin from Artocarpus hirsuta in complex with methyl-alpha-D-galactose.
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Acta Crystallogr D Biol Crystallogr,
60,
1404-1412.
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PDB codes:
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M.Goel,
P.Anuradha,
K.J.Kaur,
B.G.Maiya,
M.J.Swamy,
and
D.M.Salunke
(2004).
Porphyrin binding to jacalin is facilitated by the inherent plasticity of the carbohydrate-binding site: novel mode of lectin-ligand interaction.
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Acta Crystallogr D Biol Crystallogr,
60,
281-288.
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PDB code:
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N.Sugimori,
T.Torizawa,
D.J.Aceti,
S.Thao,
J.L.Markley,
and
M.Kainosho
(2004).
(1)H, (13)C and (15)N backbone assignment of a 32 kDa hypothetical protein from Arabidopsis thaliana, At3g16450.1.
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J Biomol NMR,
30,
357-358.
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D.H.Shin,
A.Roberts,
J.Jancarik,
H.Yokota,
R.Kim,
D.E.Wemmer,
and
S.H.Kim
(2003).
Crystal structure of a phosphatase with a unique substrate binding domain from Thermotoga maritima.
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Protein Sci,
12,
1464-1472.
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PDB code:
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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
codes are
shown on the right.
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}
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