1el4

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(New page: 200px<br /><applet load="1el4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1el4, resolution 1.73&Aring;" /> '''STRUCTURE OF THE CAL...)
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[[Image:1el4.gif|left|200px]]<br /><applet load="1el4" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1el4.gif|left|200px]]<br /><applet load="1el4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1el4, resolution 1.73&Aring;" />
caption="1el4, resolution 1.73&Aring;" />
'''STRUCTURE OF THE CALCIUM-REGULATED PHOTOPROTEIN OBELIN DETERMINED BY SULFUR SAS'''<br />
'''STRUCTURE OF THE CALCIUM-REGULATED PHOTOPROTEIN OBELIN DETERMINED BY SULFUR SAS'''<br />
==Overview==
==Overview==
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The crystal structure of the photoprotein obelin (22.2 kDa) from Obelia, longissima has been determined and refined to 1.7 A resolution. Contrary, to the prediction of a peroxide, the noncovalently bound substrate, coelenterazine, has only a single oxygen atom bound at the C2-position., The protein-coelenterazine 2-oxy complex observed in the crystals is, photo-active because, in the presence of calcium ion, bioluminescence, emission within the crystal is observed. This structure represents only, the second de novo protein structure determined using the anomalous, scattering signal of the sulfur substructure in the crystal. The method, used here is theoretically different from that used for crambin in 1981, (4.72 kDa) and represents a significant advancement in protein crystal, structure determination.
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The crystal structure of the photoprotein obelin (22.2 kDa) from Obelia longissima has been determined and refined to 1.7 A resolution. Contrary to the prediction of a peroxide, the noncovalently bound substrate, coelenterazine, has only a single oxygen atom bound at the C2-position. The protein-coelenterazine 2-oxy complex observed in the crystals is photo-active because, in the presence of calcium ion, bioluminescence emission within the crystal is observed. This structure represents only the second de novo protein structure determined using the anomalous scattering signal of the sulfur substructure in the crystal. The method used here is theoretically different from that used for crambin in 1981 (4.72 kDa) and represents a significant advancement in protein crystal structure determination.
==About this Structure==
==About this Structure==
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1EL4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Obelia_longissima Obelia longissima] with CL and CTZ as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EL4 OCA].
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1EL4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Obelia_longissima Obelia longissima] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=CTZ:'>CTZ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EL4 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Lee, J.]]
[[Category: Lee, J.]]
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[[Category: Liu, Z.J.]]
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[[Category: Liu, Z J.]]
[[Category: Rose, J.]]
[[Category: Rose, J.]]
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[[Category: Vysotski, E.S.]]
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[[Category: Vysotski, E S.]]
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[[Category: Wang, B.C.]]
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[[Category: Wang, B C.]]
[[Category: CL]]
[[Category: CL]]
[[Category: CTZ]]
[[Category: CTZ]]
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[[Category: sulfur anomalous scattering]]
[[Category: sulfur anomalous scattering]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:05:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:53 2008''

Revision as of 10:28, 21 February 2008

Image:1el4.gif

1el4, resolution 1.73Å

Drag the structure with the mouse to rotate

STRUCTURE OF THE CALCIUM-REGULATED PHOTOPROTEIN OBELIN DETERMINED BY SULFUR SAS

Overview

The crystal structure of the photoprotein obelin (22.2 kDa) from Obelia longissima has been determined and refined to 1.7 A resolution. Contrary to the prediction of a peroxide, the noncovalently bound substrate, coelenterazine, has only a single oxygen atom bound at the C2-position. The protein-coelenterazine 2-oxy complex observed in the crystals is photo-active because, in the presence of calcium ion, bioluminescence emission within the crystal is observed. This structure represents only the second de novo protein structure determined using the anomalous scattering signal of the sulfur substructure in the crystal. The method used here is theoretically different from that used for crambin in 1981 (4.72 kDa) and represents a significant advancement in protein crystal structure determination.

About this Structure

1EL4 is a Single protein structure of sequence from Obelia longissima with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the Ca2+-regulated photoprotein obelin at 1.7 A resolution determined directly from its sulfur substructure., Liu ZJ, Vysotski ES, Chen CJ, Rose JP, Lee J, Wang BC, Protein Sci. 2000 Nov;9(11):2085-93. PMID:11152120

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