Structural Characterization of Ferrous Ion Binding to Retinal Guanylate Cyclase Activator Protein 5 from Zebrafish Photoreceptors.

ABSTRACT: Sensory guanylate cyclases (zGCs) in zebrafish photoreceptors are regulated by a family of guanylate cyclase activator proteins (called GCAP1-7). GCAP5 contains two nonconserved cysteine residues (Cys15 and Cys17) that could in principle bind to biologically active transition state metal ions (Zn²⁺ and Fe²⁺). Here, we present nuclear magnetic resonance (NMR) and isothermal titration calorimetry (ITC) binding analyses that demonstrate the binding of one Fe²⁺ ion to two GCAP5 molecules (in a 1:2 complex) with a dissociation constant in the nanomolar range. At least one other Fe²⁺ binds to GCAP5 with micromolar affinity that likely represents electrostatic Fe²⁺ binding to the EF-hand loops. The GCAP5 double mutant (C15A/C17A) lacks nanomo

SUBMITTER: Lim S 

PROVIDER: S-EPMC5743585 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature