1l3r
From Proteopedia
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Crystal Structure of a Transition State Mimic of the Catalytic Subunit of cAMP-dependent Protein Kinase
Overview
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.
About this Structure
1L3R is a Protein complex structure of sequences from Mus musculus with , , and as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase., Madhusudan, Akamine P, Xuong NH, Taylor SS, Nat Struct Biol. 2002 Apr;9(4):273-7. PMID:11896404
Page seeded by OCA on Thu Feb 21 13:40:58 2008
