4IAC

X-RAY structure of cAMP dependent protein kinase A in complex with HIGH MG2+ concentration, AMP-PCP AND pseudo-substrate peptide SP20

4IAC の概要

• エントリーDOI: 10.2210/pdb4iac/pdb
• 関連するPDBエントリー: 4IAD 4IAF 4IAI 4IAK 4IAY 4IAZ 4IB0 4IB1 4IB3
• 分子名称: cAMP-dependent protein kinase catalytic subunit alpha, Peptide SP20, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: kinase, phosphorylation, auto-phosphorylated, 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: 44319.38

構造登録者

Gerlits, O.,Kovalevsky, A. (登録日: 2012-12-06, 公開日: 2013-06-12, 最終更新日: 2024-10-16)

主引用文献

Gerlits, O.,Waltman, M.J.,Taylor, S.,Langan, P.,Kovalevsky, A.
Insights into the Phosphoryl Transfer Catalyzed by cAMP-Dependent Protein Kinase: An X-ray Crystallographic Study of Complexes with Various Metals and Peptide Substrate SP20.
Biochemistry, 52:3721-3727, 2013

PubMed Abstract: X-ray structures of several ternary substrate and product complexes of the catalytic subunit of cAMP-dependent protein kinase (PKAc) have been determined with different bound metal ions. In the PKAc complexes, Mg(2+), Ca(2+), Sr(2+), and Ba(2+) metal ions could bind to the active site and facilitate the phosphoryl transfer reaction. ATP and a substrate peptide (SP20) were modified, and the reaction products ADP and the phosphorylated peptide were found trapped in the enzyme active site. Finally, we determined the structure of a pseudo-Michaelis complex containing Mg(2+), nonhydrolyzable AMP-PCP (β,γ-methyleneadenosine 5'-triphosphate) and SP20. The product structures together with the pseudo-Michaelis complex provide snapshots of different stages of the phosphorylation reaction. Comparison of these structures reveals conformational, coordination, and hydrogen bonding changes that might occur during the reaction and shed new light on its mechanism, roles of metals, and active site residues.

PubMed: 23672593
DOI: 10.1021/bi400066a

実験手法

X-RAY DIFFRACTION (2.15 Å)