6R4P

Structure of a soluble domain of adenylyl cyclase bound to an activated stimulatory G protein

6R4P の概要

• エントリーDOI: 10.2210/pdb6r4p/pdb
• EMDBエントリー: 4719 4722
• 分子名称: Adenylate cyclase 9, Guanine nucleotide-binding protein G(s) subunit alpha isoforms short, 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: membrane protein, adenylyl cyclase, g protein, occluded state
• 由来する生物種: Bos taurus (Bovine); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 229900.70

構造登録者

Korkhov, V.M.,Qi, C. (登録日: 2019-03-22, 公開日: 2019-05-08, 最終更新日: 2024-05-15)

主引用文献

Qi, C.,Sorrentino, S.,Medalia, O.,Korkhov, V.M.
The structure of a membrane adenylyl cyclase bound to an activated stimulatory G protein.
Science, 364:389-394, 2019

PubMed Abstract: Membrane-integral adenylyl cyclases (ACs) are key enzymes in mammalian heterotrimeric GTP-binding protein (G protein)-dependent signal transduction, which is important in many cellular processes. Signals received by the G protein-coupled receptors are conveyed to ACs through G proteins to modulate the levels of cellular cyclic adenosine monophosphate (cAMP). Here, we describe the cryo-electron microscopy structure of the bovine membrane AC9 bound to an activated G protein αs subunit at 3.4-angstrom resolution. The structure reveals the organization of the membrane domain and helical domain that spans between the membrane and catalytic domains of AC9. The carboxyl-terminal extension of the catalytic domain occludes both the catalytic and the allosteric sites of AC9, inducing a conformation distinct from the substrate- and activator-bound state, suggesting a regulatory role in cAMP production.

PubMed: 31023924
DOI: 10.1126/science.aav0778

実験手法

ELECTRON MICROSCOPY (3.1 Å)