Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase
Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase
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DOI：
10.1038/nsb780
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发表时间：
2002-04-01
期刊：
影响因子：
--
通讯作者：
Taylor, SS
中科院分区：
文献类型：
--
作者：
Madhusudan;Akamine, P;Taylor, SS
为了了解camp依赖性蛋白激酶磷酸化的分子机制，在2.0埃分辨率下测定了ADP、氟化铝、Mg2+离子和底物肽配合物的催化亚基结构。将氟化铝建模为平面几何形状的AlF3；距ADP的供氧和受体Ser残基的羟基均为2.3埃。在这种构型中，铝原子与供体和受体基团的氧原子在顶端位置形成三角双锥体配位。这种排列表明氟化铝模拟了过渡态，并为蛋白激酶中磷酸化转移的在线机制提供了第一个直接的结构证据。
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.