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Structure of the Ca2+-regulated photoprotein obelin at 1.7 Å resolution determined directly from its sulfur substructure

Published online by Cambridge University Press:  15 December 2000

ZHI-JIE LIU ,
EUGENE S. VYSOTSKI ,
CHUN-JUNG CHEN ,
JOHN P. ROSE ,
JOHN LEE  and
BI-CHENG WANG
ZHI-JIE LIU
Affiliation:
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602
EUGENE S. VYSOTSKI
Affiliation:
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602 Institute of Biophysics, RAS (SB), Krasnoyarsk 660036, Russia
CHUN-JUNG CHEN
Affiliation:
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602
JOHN P. ROSE
Affiliation:
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602
JOHN LEE
Affiliation:
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602
BI-CHENG WANG
Affiliation:
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602
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Abstract

The crystal structure of the photoprotein obelin (22.2 kDa) from Obelia longissima has been determined and refined to 1.7 Å 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.

Keywords

bioluminescencecrystallographyobelinphotoproteinsingle wavelength anomalous scatteringsolvent flatteningsulfur phasing
Type
Research Article
Information
Protein Science , Volume 9 , Issue 11 , November 2000 , pp. 2085 - 2093
Copyright
2000 The Protein Society

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