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首页> 美国卫生研究院文献>The Journal of Biological Chemistry >Probing Open Conformation of GroEL Rings by Cross-linking Reveals Single and Double Open Ring Structures of GroEL in ADP and ATP
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Probing Open Conformation of GroEL Rings by Cross-linking Reveals Single and Double Open Ring Structures of GroEL in ADP and ATP

机译：通过交联探测GroEL环的开环构象揭示了ADP和ATP中GroEL的单和双开环结构

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摘要

Two heptamer rings of chaperonin GroEL undergo opening-closing conformational transition in the reaction cycle with the aid of GroES and ATP. We introduced Cys into the GroEL subunit at Ala-384 and Ser-509, which are very close between adjacent GroEL subunits in the open heptamer ring but far apart in the closed heptamer ring. The open ring-specific inter-subunit cross-linking between these Cys indicated that the number of rings in open conformation in GroEL was two in ATP (GroELOO), one in ADP (GroELO), and none in the absence of nucleotide. ADP showed an inhibitory effect on ATP-induced generation of GroELOO. The isolated GroELO and GroELOO, which lost any bound nucleotide, could bind GroES to form a bullet-shaped 1:1 GroEL-GroES complex and a football-shaped 1:2 GroEL-GroES complex, respectively, even without the addition of any nucleotide. Substrate protein was unable to form a stable complex with GroELOO and did not stimulate ATPase activity of GroEL. These results favor a model of the GroEL reaction cycle that includes a football complex as a critical intermediate.
机译：伴侣蛋白GroEL的两个七聚体环在反应循环中借助GroES和ATP进行开-关构象转变。我们将Cys引入Ala-384和Ser-509的GroEL亚基中，它们在开放的七聚体环中相邻的GroEL亚基之间非常接近，而在封闭的七聚体环中相距很远。这些Cys之间的开环特异性亚基间交联表明，GroEL中呈开放构象的环数在ATP（GroELOO）中为两个，在ADP（GroELO）中为一个，在没有核苷酸的情况下没有。 ADP对ATP诱导的GroELOO生成具有抑制作用。分离的GroELO和GroELOO丢失了任何结合的核苷酸，即使不添加任何核苷酸，也可以结合GroES形成子弹形的1：1 GroEL-GroES复合物和橄榄球形的1：2 GroEL-GroES复合物。 。底物蛋白无法与GroELOO形成稳定的复合物，并且不会刺激GroEL的ATPase活性。这些结果有利于GroEL反应周期的模型，该模型包括足球场作为关键的中间体。

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