1ij5

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(New page: 200px<br /><applet load="1ij5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ij5, resolution 3.0&Aring;" /> '''METAL-FREE STRUCTURE ...)
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[[Image:1ij5.gif|left|200px]]<br /><applet load="1ij5" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ij5, resolution 3.0&Aring;" />
caption="1ij5, resolution 3.0&Aring;" />
'''METAL-FREE STRUCTURE OF MULTIDOMAIN EF-HAND PROTEIN, CBP40, FROM TRUE SLIME MOLD'''<br />
'''METAL-FREE STRUCTURE OF MULTIDOMAIN EF-HAND PROTEIN, CBP40, FROM TRUE SLIME MOLD'''<br />
==Overview==
==Overview==
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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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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.
==About this Structure==
==About this Structure==
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1IJ5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physarum_polycephalum Physarum polycephalum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IJ5 OCA].
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1IJ5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physarum_polycephalum Physarum polycephalum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJ5 OCA].
==Reference==
==Reference==
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[[Category: fourty kda calcium binding protein]]
[[Category: fourty kda calcium binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:26:28 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:23 2008''

Revision as of 11:12, 21 February 2008


1ij5, resolution 3.0Å

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METAL-FREE STRUCTURE OF MULTIDOMAIN EF-HAND PROTEIN, CBP40, FROM TRUE SLIME MOLD

Overview

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.

About this Structure

1IJ5 is a Single protein structure of sequence from Physarum polycephalum. Full crystallographic information is available from OCA.

Reference

Metal-free and Ca2+-bound structures of a multidomain EF-hand protein, CBP40, from the lower eukaryote Physarum polycephalum., Iwasaki W, Sasaki H, Nakamura A, Kohama K, Tanokura M, Structure. 2003 Jan;11(1):75-85. PMID:12517342

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