分子伴侣GroE系统能量传递机制的研究

用SwissPDBViewer软件对分子伴侣GroE系统与底物的相互作用进行了模拟 ,结果表明 :GroEL顶端结构域在GroES和靶蛋白结合之后发生了明显的变化 ;GroEL的cis环上有与三磷酸腺苷ATP相结合的位点 ,ATP水解之后形成的ADP与活性中心的残基相结合 ,而这种结合除导致残基Thr30的构型发生了变化之外 ,其它残基的空间位置和构型基本保持不变 ,暗示其它残基在能量传递过程中形成了刚性骨架 ,而与ADP分子磷酸键结合的残基Thr30则是能量传递的力点。

Researches on Energy Transfer Mechanism of Molecular Chaperone GroE

Modeling of interactions between molecular chaperone GroE and its substrate was studied by software SwissPDBViewer. The results showed that the GroEL apical domain changed a lot when GroES or substrate bound to it. There were ATP binding sites in the cis ring of GroEL. When ATP hydrolyzed to ADP which bound to residues in active sites, the conformation of residue Thr30 changed, but other residues remained invariable. It implied that other residues in the active sites formed a rigid framework during the energy transferring process, but the residue Thr30 is the key point of energy transferring.