4IAI

X-ray Structure of cAMP dependent protein kinase A in complex with high Ca2+ concentration, ADP and phosphorylated peptide pSP20

Summary for 4IAI

• Entry DOI: 10.2210/pdb4iai/pdb
• Related: 4IAC 4IAD 4IAF 4IAK 4IAY 4IAZ 4IB0 4IB1 4IB3
• Descriptor: cAMP-dependent protein kinase catalytic subunit alpha, phosphorylated pseudo-substrate peptide pSP20, CALCIUM ION, ... (7 entities in total)
• Functional Keywords: kinase enzyme, phosphotransfer, phosphorylation, transferase-peptide complex, transferase/peptide
• Biological source: Mus musculus (mouse); More
• Cellular location: Cytoplasm. Isoform 2: Cell projection, cilium, flagellum (By similarity): P05132
• Total number of polymer chains: 2
• Total formula weight: 44519.02

Authors

Gerlits, O.,Kovalevsky, A. (deposition date: 2012-12-06, release date: 2013-06-12, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.55 Å)