1L3R

Crystal Structure of a Transition State Mimic of the Catalytic Subunit of cAMP-dependent Protein Kinase

Summary for 1L3R

• Entry DOI: 10.2210/pdb1l3r/pdb
• Related: 1APM 1ATP 1JBP
• Descriptor: CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT, CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, MUSCLE/BRAIN FORM, MAGNESIUM ION, ... (7 entities in total)
• Functional Keywords: protein kinase, protein-alf3 complex, transition state mimic, transferase
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cytoplasm (By similarity): P05132
• Total number of polymer chains: 2
• Total formula weight: 43694.62

Authors

Madhusudan,Akamine, P.,Xuong, N.-H.,Taylor, S.S. (deposition date: 2002-02-28, release date: 2002-03-20, Last modification date: 2024-10-16)

Primary citation

Madhusudan,Akamine, P.,Xuong, N.H.,Taylor, S.S.
Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase.
Nat.Struct.Biol., 9:273-277, 2002

PubMed Abstract: To understand the molecular mechanism underlying phosphoryl transfer of cAMP-dependent protein kinase, the structure of the catalytic subunit in complex with ADP, aluminum fluoride, Mg2+ ions and a substrate peptide was determined at 2.0 A resolution. Aluminum fluoride was modeled as AlF3 in a planar geometry; it is positioned 2.3 A from both the donor oxygen of ADP and the hydroxyl group of the recipient Ser residue. In this configuration, the aluminum atom forms a trigonal bipyramidal coordination with the oxygen atoms of the donor and recipient groups at the apical positions. This arrangement suggests that aluminum fluoride mimics the transition state and provides the first direct structural evidence for the in-line mechanism of phosphoryl transfer in a protein kinase.

PubMed: 11896404
DOI: 10.1038/nsb780

Experimental method

X-RAY DIFFRACTION (2 Å)