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PDBsum entry 1con
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Lectin(agglutinin)
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PDB id
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1con
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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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Refined structure of cadmium-Substituted concanavalin a at 2.0 a resolution.
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Authors
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J.H.Naismith,
J.Habash,
S.Harrop,
J.R.Helliwell,
W.N.Hunter,
T.C.Wan,
S.Weisgerber,
A.J.Kalb,
J.Yariv.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1993,
49,
561-571.
[DOI no: ]
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PubMed id
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Abstract
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The three-dimensional structure of cadmium-substituted concanavalin A has been
refined using X-PLOR. The R factor on all data between 8 and 2 A is 17.1%. The
protein crystallizes in space group I222 with cell dimensions a = 88.7, b = 86.5
and c = 62.5 A and has one protein subunit per asymmetric unit. The final
structure contains 237 amino acids, two Cd ions, one Ca ion and 144 water
molecules. One Cd ion occupies the transition-metal binding site and the second
occupies an additional site, the coordinates of which were first reported by
Weinzierl & Kalb [FEBS Lett. (1971), 18, 268-270]. The additional Cd ion is
bound with distorted octahedral symmetry and bridges the cleft between the two
monomers which form the conventional dimer of concanavalin A. This study
provides a detailed analysis of the refined structure of saccharide-free
concanavalin A and is the basis for comparison with saccharide complexes
reported elsewhere.
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Figure 5.
Fig. 5. The tetramer of concanavalin A viewed down a molecular
twofold axis.
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Figure 6.
Fig. 6. The
S1 (Ca 2+)
and
$2 (Cd 2+)
metal sites. Both sites have
octahedral-like geometry with Aspl0 capping an axial position
of the Ca 2÷ ion. Aspl9 and Aspl0 are bound to both metals.
Asp208
is shown and it makes hydrogen bonds with
WC
which
are thought to stabilize the
cis
peptide. The two metal ions are
separated
by 4.18/~,.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1993,
49,
561-571)
copyright 1993.
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Secondary reference #1
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Title
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Non-Glycosylated recombinant pro-Concanavalin a is active without polypeptide cleavage.
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Authors
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W.Min,
A.J.Dunn,
D.H.Jones.
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Ref.
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Embo J, 1992,
11,
1303-1307.
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PubMed id
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