NMR and EPR-DEER Structure of a Dimeric Guanylate Cyclase Activator Protein-5 from Zebrafish Photoreceptors.

ABSTRACT: Retinal guanylate cyclases (RetGCs) are regulated by a family of guanylate cyclase-activating proteins (called GCAP1-7). GCAPs form dimers that bind to Ca²⁺ and confer Ca²⁺ sensitive activation of RetGC during visual phototransduction. The GCAP5 homologue from zebrafish contains two nonconserved cysteine residues (Cys15 and Cys17) that bind to ferrous ion, which stabilizes GCAP5 dimerization and diminishes its ability to activate RetGC. Here, we present NMR and EPR-DEER structural analysis of a GCAP5 dimer in the Mg²⁺-bound, Ca²⁺-free, Fe²⁺-free activator state. The NMR-derived structure of GCAP5 is similar to the crystal structure of Ca²⁺-bound GCAP1 (root-mean-square deviation of 2.4 Å), except that the N-terminal helix of

SUBMITTER: Cudia D 

PROVIDER: S-EPMC8944188 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature