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J Biol Chem, Vol. 274, Issue 27, 19329-19337, July 2, 1999

Three-dimensional Structure of Guanylyl Cyclase Activating Protein-2, a Calcium-sensitive Modulator of Photoreceptor Guanylyl Cyclases

James B. AmesDagger , Alexander M. Dizhoor, Mitsuhiko Ikura**, Krzysztof Palczewski§§, and Lubert Stryer||

From the Dagger  Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850,  Department of Ophthalmology/Kresge Eye Institute, Wayne State University School of Medicine, Detroit, Michigan 48201, ** Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada M5G 2M9, §§ Departments of Ophthalmology, Pharmacology, and Chemistry, University of Washington, Seattle, Washington 98195, and the || Department of Neurobiology, Stanford University School of Medicine, Stanford, California 94305-5125

Guanylyl cyclase activating protein-2 (GCAP-2) is a Ca2+-sensitive regulator of phototransduction in retinal photoreceptor cells. GCAP-2 activates retinal guanylyl cyclases at low Ca2+ concentration (<100 nM) and inhibits them at high Ca2+ (>500 nM). The light-induced lowering of the Ca2+ level from ~500 nM in the dark to ~50 nM following illumination is known to play a key role in visual recovery and adaptation. We report here the three-dimensional structure of unmyristoylated GCAP-2 with three bound Ca2+ ions as determined by nuclear magnetic resonance spectroscopy of recombinant, isotopically labeled protein. GCAP-2 contains four EF-hand motifs arranged in a compact tandem array like that seen previously in recoverin. The root mean square deviation of the main chain atoms in the EF-hand regions is 2.2 Å in comparing the Ca2+-bound structures of GCAP-2 and recoverin. EF-1, as in recoverin, does not bind calcium because it contains a disabling Cys-Pro sequence. GCAP-2 differs from recoverin in that the calcium ion binds to EF-4 in addition to EF-2 and EF-3. A prominent exposed patch of hydrophobic residues formed by EF-1 and EF-2 (Leu24, Trp27, Phe31, Phe45, Phe48, Phe49, Tyr81, Val82, Leu85, and Leu89) may serve as a target-binding site for the transmission of calcium signals to guanylyl cyclase.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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