Journal
NATURE STRUCTURAL BIOLOGY
Volume 9, Issue 4, Pages 273-277Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsb780
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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 Angstrom resolution. Aluminum fluoride was modeled as AlF3 in a planar geometry; it is positioned 2.3 Angstrom 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.
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