1CJV

COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP, MG, AND ZN

1CJV の概要

• エントリーDOI: 10.2210/pdb1cjv/pdb
• 分子名称: ADENYLATE CYCLASE, TYPE V, 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE, ADENYLATE CYCLASE, TYPE II, ... (11 entities in total)
• 機能のキーワード: complex (lyase-hydrolase), hydrolase, signal transducing protein, cyclase, effector enzyme, lyase-lyase-signaling protein complex, lyase/lyase/signaling protein
• 由来する生物種: Canis lupus familiaris (dog); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 96703.88

構造登録者

Tesmer, J.J.G.,Sprang, S.R. (登録日: 1999-04-19, 公開日: 1999-08-31, 最終更新日: 2023-09-20)

主引用文献

Tesmer, J.J.,Sunahara, R.K.,Johnson, R.A.,Gosselin, G.,Gilman, A.G.,Sprang, S.R.
Two-metal-Ion catalysis in adenylyl cyclase.
Science, 285:756-760, 1999

PubMed Abstract: Adenylyl cyclase (AC) converts adenosine triphosphate (ATP) to cyclic adenosine monophosphate, a ubiquitous second messenger that regulates many cellular functions. Recent structural studies have revealed much about the structure and function of mammalian AC but have not fully defined its active site or catalytic mechanism. Four crystal structures were determined of the catalytic domains of AC in complex with two different ATP analogs and various divalent metal ions. These structures provide a model for the enzyme-substrate complex and conclusively demonstrate that two metal ions bind in the active site. The similarity of the active site of AC to those of DNA polymerases suggests that the enzymes catalyze phosphoryl transfer by the same two-metal-ion mechanism and likely have evolved from a common ancestor.

PubMed: 10427002
DOI: 10.1126/science.285.5428.756

実験手法

X-RAY DIFFRACTION (3 Å)