A proline switch controls folding and domain interactions in the gene-3-protein of the filamentous phage fd.
A proline switch controls folding and domain interactions in the gene-3-protein of the filamentous phage fd.
复制标题
脯氨酸开关控制丝状噬菌体 fd 基因 3 蛋白中的折叠和结构域相互作用。
DOI：
10.1016/s0022-2836(03)00864-7
复制
发表时间：
2003
影响因子：
5.6
通讯作者：
F. Schmid
中科院分区：
文献类型：
--
作者：
Andreas Martin;F. Schmid
噬菌体Fd基因-3蛋白的氨基末端结构域N1和N2形成一个从噬菌体末端伸出的双叶结构和功能实体。结构域n2通过与F菌毛结合而启动对大肠杆菌的感染。这种结合导致两个结构域的解离，并允许N1与细胞表面的TOLA受体相互作用。N1-N2片段的重折叠开始于结构域N1的折叠，这需要几毫秒，然后是结构域N2的折叠，其在5分钟内完成。随后的结构域组装异常缓慢，在25℃时，S的时间常数为6200。我们发现，这个反应的速度是由N2铰链亚结构域中Gln212-Pro213键的反式异构化控制的，该区域提供了基因-3-蛋白中N1和N2之间的许多相互作用。用Gly取代Pro213，使结构域结合加速了30倍，揭示了这两个单独结构域的折叠及其组装确实是基因-3-蛋白重折叠的连续步骤。在感染过程中，结构域必须分离，以暴露N1结构域上的TOLA结合位点。Pro213异构化引起的结构域重组的动力学障碍可以确保在N2与F菌毛的初始结合后，开放状态一直持续到N1和TOLA足够接近相互作用为止。因此，Pro213异构化可能是基因-3蛋白功能的一种缓慢的构象转换。
The amino-terminal domains N1 and N2 of the gene-3-protein of phage fd form a bilobal structural and functional entity that protrudes from the phage tip. Domain N2 initiates the infection of Escherichia coli by binding to the F pilus. This binding results in the dissociation of the two domains and allows N1 to interact with the TolA receptor at the cell surface. The refolding of the N1–N2 fragment begins with the folding of domain N1, which takes a few milliseconds, followed by the folding of domain N2, which is complete within five minutes. The subsequent domain assembly is unusually slow and shows a time-constant of 6200 s at 25 °C. We found that the rate of this reaction is controlled by the trans to cis isomerization of the Gln212-Pro213 bond in the hinge subdomain of N2, a region that provides many interactions between N1 and N2 in the gene-3-protein. The substitution of Pro213 by Gly accelerated domain association 30-fold and revealed that the folding of the two individual domains and their assembly are indeed sequential steps in the refolding of the gene-3-protein. In the course of infection, the domains must separate to expose the binding site for TolA on domain N1. The kinetic block of domain reassembly caused by Pro213 isomerization could ensure that after the initial binding of N2 to the F pilus the open state persists until N1 and TolA are close enough for their mutual interaction. Pro213 isomerization might thus serve as a slow conformational switch in the function of the gene-3-protein.
酵母 iso-2 细胞色素 c 中的缓慢重折叠动力学。
影响因子：
2.9
作者：
OsterhoutJr,JJ;Nall,BT
通讯作者：
Nall,BT
蛋白质果胶酸裂解酶 C 的折叠动力学揭示了快速形成的中间体和缓慢的脯氨酸异构化。
影响因子：
2.9
作者：
Kamen,DouglasE;Woody,RobertW
通讯作者：
Woody,RobertW
影响因子：
56.9
作者：
Yaffe, MB;Schutkowski, M;Lu, KP
通讯作者：
Lu, KP