7MY4

Crystal Structure of the SPA17 Docking and Dimerization Domain from Danio rerio

7MY4 の概要

• エントリーDOI: 10.2210/pdb7my4/pdb
• 分子名称: Sperm autoantigenic protein 17 (2 entities in total)
• 機能のキーワード: oligomerization, a-kinase anchoring protein (akap) binding domain, protein binding
• 由来する生物種: Danio rerio (Zebrafish, Brachydanio rerio)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 33653.63

構造登録者

Dahlin, H.R.,Zheng, N. (登録日: 2021-05-20, 公開日: 2021-05-26, 最終更新日: 2023-10-18)

主引用文献

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

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: 34256050
DOI: 10.1016/j.jbc.2021.100927

実験手法

X-RAY DIFFRACTION (1.72 Å)