Bochkareva E S, Girshovich A S
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
J Biol Chem. 1994 Sep 30;269(39):23869-71.
For its function, the Escherichia coli chaperonin GroEL requires the presence of ATP and co-chaperonin GroES. We have observed that ADP displays a two-step inhibition of GroEL-dependent ATP hydrolysis, wherein one-half of the GroEL ATPase sites is strongly inhibited by ADP while the other half is affected very mildly. It is suggested that interaction with ATP induces structural and functional differences between two initially identical rings in GroEL (inter-ring negative cooperativity) and that the subsequent binding of GroES occurs to the ring that is occupied first by ATP in a positively cooperative manner.
就其功能而言，大肠杆菌伴侣蛋白GroEL需要ATP和共伴侣蛋白GroES的存在。我们观察到，ADP对GroEL依赖的ATP水解表现出两步抑制作用，其中一半的GroEL ATP酶位点被ADP强烈抑制，而另一半受到的影响非常轻微。有人认为，与ATP的相互作用会诱导GroEL中两个最初相同的环之间的结构和功能差异（环间负协同性），随后GroES以正协同方式与首先被ATP占据的环结合。
