7MY4
Crystal Structure of the SPA17 Docking and Dimerization Domain from Danio rerio
Summary for 7MY4
| Entry DOI | 10.2210/pdb7my4/pdb |
| Descriptor | Sperm autoantigenic protein 17 (2 entities in total) |
| Functional Keywords | oligomerization, a-kinase anchoring protein (akap) binding domain, protein binding |
| Biological source | Danio rerio (Zebrafish, Brachydanio rerio) |
| Total number of polymer chains | 4 |
| Total formula weight | 33653.63 |
| Authors | Dahlin, H.R.,Zheng, N. (deposition date: 2021-05-20, release date: 2021-05-26, Last modification date: 2023-10-18) |
| Primary citation | Dahlin, H.R.,Zheng, N.,Scott, J.D. Beyond PKA: Evolutionary and structural insights that define a docking and dimerization domain superfamily. J.Biol.Chem., 297:100927-100927, 2021 Cited by PubMed Abstract: Protein-interaction domains can create unique macromolecular complexes that drive evolutionary innovation. By combining bioinformatic and phylogenetic analyses with structural approaches, we have discovered that the docking and dimerization (D/D) domain of the PKA regulatory subunit is an ancient and conserved protein fold. An archetypal function of this module is to interact with A-kinase-anchoring proteins (AKAPs) that facilitate compartmentalization of this key cell-signaling enzyme. Homology searching reveals that D/D domain proteins comprise a superfamily with 18 members that function in a variety of molecular and cellular contexts. Further in silico analyses indicate that D/D domains segregate into subgroups on the basis of their similarity to type I or type II PKA regulatory subunits. The sperm autoantigenic protein 17 (SPA17) is a prototype of the type II or R2D2 subgroup that is conserved across metazoan phyla. We determined the crystal structure of an extended D/D domain from SPA17 (amino acids 1-75) at 1.72 Å resolution. This revealed a four-helix bundle-like configuration featuring terminal β-strands that can mediate higher order oligomerization. In solution, SPA17 forms both homodimers and tetramers and displays a weak affinity for AKAP18. Quantitative approaches reveal that AKAP18 binding occurs at nanomolar affinity when SPA17 heterodimerizes with the ropporin-1-like D/D protein. These findings expand the role of the D/D fold as a versatile protein-interaction element that maintains the integrity of macromolecular architectures within organelles such as motile cilia. PubMed: 34256050DOI: 10.1016/j.jbc.2021.100927 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.72 Å) |
Structure validation
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