STRUCTURAL BASIS OF THE ALLOSTERIC BEHAVIOR OF PHOSPHOFRUCTOKINASE
STRUCTURAL BASIS OF THE ALLOSTERIC BEHAVIOR OF PHOSPHOFRUCTOKINASE
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DOI：
10.1038/343140a0
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发表时间：
1990-01-11
期刊：
影响因子：
64.8
通讯作者：
EVANS, PR
中科院分区：
文献类型：
--
作者：
SCHIRMER, T;EVANS, PR
磷酸果糖激酶低亲和力形式和高亲和力形式的晶体结构之间的比较表明，四级结构的变化与变构效应子结合引发的局部变化之间存在紧密耦合。这些协调一致的变化将四聚体中的所有底物和效应位点连接起来，并解释了对协同底物的亲和力的变化。
Comparison between the crystal structures of low-and high-affinity forms of phosphofructokinase shows a close coupling between the change of quaternary structure and local changes triggered by binding of the allosteric effectors. These concerted changes link all the substrate and effector sites in the tetramer, and explain the change of affinity for the cooperative substrate.