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PDBsum entry 1ij6
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Metal binding protein
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PDB id
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1ij6
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References listed in PDB file
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Key reference
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Title
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Metal-Free and ca2+-Bound structures of a multidomain ef-Hand protein, Cbp40, From the lower eukaryote physarum polycephalum.
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Authors
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W.Iwasaki,
H.Sasaki,
A.Nakamura,
K.Kohama,
M.Tanokura.
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Ref.
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Structure, 2003,
11,
75-85.
[DOI no: ]
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PubMed id
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Abstract
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Acellular slime mold, Physarum polycephalum, has a unique wound-healing system.
When cytoplasm of plasmodia is exposed to extracellular fluid, calcium binding
protein 40 (CBP40) seals damaged areas, forming large aggregates Ca(2+)
dependently. Part of the CBP40 is truncated at the N terminus by a proteinase in
plasmodia (CBP40delta), which does not aggregate in the Ca(2+)-bound form. Here
we report the crystal structures of CBP40delta in both the metal-free and the
Ca(2+)-bound states. Both structures consist of three domains: coiled-coil,
intervening, and EF-hand. The topology of the EF-hand domain is similar to that
of calpain. The N-terminal half of CBP40Delta interacts with the C-terminal
EF-hands through a large hydrophobic interface, necessary for high Ca(2+)
affinity. Conformational change upon Ca(2+) binding is small; however, the
structure of CBP40delta provides novel insights into the mechanism of
Ca(2+)-dependent oligomerization.
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Figure 6.
Figure 6. Comparison of the Interhelical Angles between the
E and F Helices of EF-HandsThe metal-free and Ca^2+-bound forms
of CBP40D are shown in yellow and white, respectively. EF3 of
Ca^2+-bound calmodulin in the open form is colored in green, and
that of Ca^2+-free calmodulin in the closed form is in red. The
Ca^2+ ions are represented as spheres in the respective backbone
colors.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2003,
11,
75-85)
copyright 2003.
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