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X-ray crystal structure of arrestin from bovine rod outer segments

Nature volume 391, pages 918–921 (1998)Cite this article

Abstract

Retinal arrestin is the essential protein for the termination of the light response in vertebrate rod outer segments. It plays an important role in quenching the light-induced enzyme cascade by its ability to bind to phosphorylated light-activated rhodopsin (P-Rh*). Arrestins are found in various G-protein-coupled amplification cascades. Here we report on the three-dimensional structure of bovine arrestin (relative molecular mass, 45,300) at 3.3 Å resolution. The crystal structure comprises two domains of antiparallel β-sheets connected through a hinge region and one short α-helix on the back of the amino-terminal fold. The binding region for phosphorylated light-activated rhodopsin is located at the N-terminal domain, as indicated by the docking of the photoreceptor to the three-dimensional structure of arrestin. This agrees with the interpretation of binding studies on partially digested and mutated arrestin.

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Figure 1: Cα-backbone of the four molecules (A, B, C, D) showing their packing in the asymmetric unit.
Figure 2: Structure of molecule B.
Figure 3
Figure 4: Possible coordination of arrestin (molecule B) and the receptor (theoretical model of metarhodopsin II23, Protein Data Bank id: 1boj, entry without loops).

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Acknowledgements

We thank A. Cousin and R. Esser for the arrestin protein preparation from bovine eyes; L. A. Donoso for the arrestin antibodies; U. B. Kaupp for continuous support of the project; K.-P. Hofmann and M. J. Lohse for helpful discussions. This work was funded by a grant from the Deutsche Forschungsgemeinschaft.

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Author notes

  1. Joachim Granzin, Ursula Wilden, Jörg Labahn, Bianca Krafft & Georg Büldt

    Present address: Department of Chemistry, Natural Science College, Chonbuk National University, 560-756, Chonju, S. Korea

  2. Joachim Granzin: Correspondence and requests for materials should be addressed to J.G. Coordinates have been deposited in the Brook haven Prote in Data Bank(accessionnumber1ayr).

Authors and Affiliations

  1. Forschungszentrum Jülich, Institut für Biologische Informationsverarbeitung, D-52425, Jülich, Germany

    Joachim Granzin & Hui-Woog Choe

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Correspondence to Joachim Granzin.

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Granzin, J., Wilden, U., Choe, HW. et al. X-ray crystal structure of arrestin from bovine rod outer segments. Nature 391, 918–921 (1998). https://doi.org/10.1038/36147

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