1el4
From Proteopedia
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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
Page seeded by OCA on Thu Feb 21 12:28:53 2008
Categories: Obelia longissima | Single protein | Lee, J. | Liu, Z J. | Rose, J. | Vysotski, E S. | Wang, B C. | CL | CTZ | Bioluminescence | Calcium | Obelin | Photoprotein | Sulfur anomalous scattering
