3X2V

Michaelis-like complex of cAMP-dependent Protein Kinase Catalytic Subunit

3X2V の概要

• エントリーDOI: 10.2210/pdb3x2v/pdb
• 関連するPDBエントリー: 3X2U 3X2W
• 分子名称: cAMP-dependent protein kinase catalytic subunit alpha, Substrate Peptide, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: michaelis-like complex, protein-substrate, pkac-atpmg2 ternary, ser/thr kinase, atp binding, phosphorylation, transferase-peptide complex, transferase/peptide
• 由来する生物種: Mus musculus (mouse); 詳細
• 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: 44512.55

構造登録者

Das, A.,Langan, P.,Gerlits, O.,Kovalevsky, A.Y.,Heller, W.T. (登録日: 2015-01-02, 公開日: 2015-12-16, 最終更新日: 2024-10-09)

主引用文献

Das, A.,Gerlits, O.,Parks, J.M.,Langan, P.,Kovalevsky, A.,Heller, W.T.
Protein Kinase A Catalytic Subunit Primed for Action: Time-Lapse Crystallography of Michaelis Complex Formation.
Structure, 23:2331-2340, 2015

PubMed Abstract: The catalytic subunit of the cyclic AMP-dependent protein kinase A (PKAc) catalyzes the transfer of the γ-phosphate of bound Mg2ATP to a serine or threonine residue of a protein substrate. Here, time-lapse X-ray crystallography was used to capture a series of complexes of PKAc with an oligopeptide substrate and unreacted Mg2ATP, including the Michaelis complex, that reveal important geometric rearrangements in and near the active site preceding the phosphoryl transfer reaction. Contrary to the prevailing view, Mg(2+) binds first to the M1 site as a complex with ATP and is followed by Mg(2+) binding to the M2 site. Concurrently, the target serine hydroxyl of the peptide substrate rotates away from the active site toward the bulk solvent, which breaks the hydrogen bond with D166. Lastly, the serine hydroxyl of the substrate rotates back toward D166 to form the Michaelis complex with the active site primed for phosphoryl transfer.

PubMed: 26585512
DOI: 10.1016/j.str.2015.10.005

実験手法

X-RAY DIFFRACTION (1.77 Å)