6MZB

Cryo-EM structure of phosphodiesterase 6

6MZB の概要

• エントリーDOI: 10.2210/pdb6mzb/pdb
• EMDBエントリー: 9297
• 分子名称: Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta, Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha, Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma, ... (6 entities in total)
• 機能のキーワード: gaf domain, phosphohydrolase, g protein-coupled receptor signaling, signaling protein
• 由来する生物種: Bos taurus (Bovine); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 218149.73

構造登録者

Gulati, S.,Palczewski, K. (登録日: 2018-11-04, 公開日: 2019-03-06, 最終更新日: 2024-10-09)

主引用文献

Gulati, S.,Palczewski, K.,Engel, A.,Stahlberg, H.,Kovacik, L.
Cryo-EM structure of phosphodiesterase 6 reveals insights into the allosteric regulation of type I phosphodiesterases.
Sci Adv, 5:eaav4322-eaav4322, 2019

PubMed Abstract: Cyclic nucleotide phosphodiesterases (PDEs) work in conjunction with adenylate/guanylate cyclases to regulate the key second messengers of G protein-coupled receptor signaling. Previous attempts to determine the full-length structure of PDE family members at high-resolution have been hindered by structural flexibility, especially in their linker regions and N- and C-terminal ends. Therefore, most structure-activity relationship studies have so far focused on truncated and conserved catalytic domains rather than the regulatory domains that allosterically govern the activity of most PDEs. Here, we used single-particle cryo-electron microscopy to determine the structure of the full-length PDE6αβ2γ complex. The final density map resolved at 3.4 Å reveals several previously unseen structural features, including a coiled N-terminal domain and the interface of PDE6γ subunits with the PDE6αβ heterodimer. Comparison of the PDE6αβ2γ complex with the closed state of PDE2A sheds light on the conformational changes associated with the allosteric activation of type I PDEs.

PubMed: 30820458
DOI: 10.1126/sciadv.aav4322

実験手法

ELECTRON MICROSCOPY (3.4 Å)