4NTT

Structure of the catalytic subunit of cAMP-dependent protein kinase bound to ADP and one magnesium ion

4NTT の概要

• エントリーDOI: 10.2210/pdb4ntt/pdb
• 関連するPDBエントリー: 1ATP 1CMK 1J3H 1SYK 4NTS
• 分子名称: cAMP-dependent protein kinase catalytic subunit alpha, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: protein kinase fold, kinase, transferase
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Cytoplasm . Isoform 2: Cell projection, cilium, flagellum : P05132
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82165.57

構造登録者

Bastidas, A.C.,Wu, J.,Taylor, S.S. (登録日: 2013-12-02, 公開日: 2014-10-15, 最終更新日: 2024-11-06)

主引用文献

Bastidas, A.C.,Wu, J.,Taylor, S.S.
Molecular Features of Product Release for the PKA Catalytic Cycle.
Biochemistry, 54:2-10, 2015

PubMed Abstract: Although ADP release is the rate limiting step in product turnover by protein kinase A, the steps and motions involved in this process are not well resolved. Here we report the apo and ADP bound structures of the myristylated catalytic subunit of PKA at 2.9 and 3.5 Å resolution, respectively. The ADP bound structure adopts a conformation that does not conform to the previously characterized open, closed, or intermediate states. In the ADP bound structure, the C-terminal tail and Gly-rich loop are more closed than in the open state adopted in the apo structure but are also much more open than the intermediate or closed conformations. Furthermore, ADP binds at the active site with only one magnesium ion, termed Mg2 from previous structures. These structures thus support a model where ADP release proceeds through release of the substrate and Mg1 followed by lifting of the Gly-rich loop and disengagement of the C-terminal tail. Coupling of these two structural elements with the release of the first metal ion fills in a key step in the catalytic cycle that has been missing and supports an ensemble of correlated conformational states that mediate the full catalytic cycle for a protein kinase.

PubMed: 25077557
DOI: 10.1021/bi500684c

実験手法

X-RAY DIFFRACTION (3.5 Å)