FIGURE

Fig. 8

ID

ZDB-FIG-221127-49

Publication

Cudia et al., 2021 - NMR and EPR-DEER Structure of a Dimeric Guanylate Cyclase Activator Protein-5 from Zebrafish Photoreceptors

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Fig. 8

Fe²⁺-dependent structural changes in GCAP5. Schematic model of dimeric GCAP5 in the Fe²⁺-free activator state (left) and Fe²⁺-bound inactive state (right). A single bound Fe²⁺ is chelated by sulfhydryl side chains of Cys15 and Cys17 from both protein subunits of the GCAP5 dimer. The intermolecular distance between the Cys15 sulfhydryl group is depicted by a double arrow. GCAP5 residues (H18, Y21, M25, F73, V76, and W93) implicated previously in the binding to guanylate cyclase^54,55 are represented by red ovals, and the putative cyclase binding site is shown by a dotted circle.

Expression Data

Expression Detail

Antibody Labeling

Phenotype Data

Phenotype Detail

Acknowledgments

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