National Institute of Technology (KOSEN), Wakayama College, 77 Noshima, Gobo, Wakayama 644-0023, Japan.
Department of Applied Chemistry and Bioscience, Graduate School of Engineering, Kanagawa Institute of Technology, 1030 Shimo-ogino, Atsugi, Kanagawa 243-0292, Japan.
J Biosci Bioeng. 2024 Oct;138(4):283-289. doi: 10.1016/j.jbiosc.2024.07.002. Epub 2024 Aug 2.
GroEL, a chaperone protein responsible for peptide and denatured protein folding, undergoes substantial conformational changes driven by ATP binding and hydrolysis during folding. Utilizing these conformational changes, we demonstrated the GroEL-mediated regioselective photocyclodimerization of 2-anthracenecarboxylic acid (AC) using ATP hydrolysis as an external stimulus. We designed and prepared an optimal GroEL mutant to employ in a docking simulation that has been actively used in recent years. Based on the large difference in the motif of hydrogen bonds between AC and GroEL mutant compared with the wild-type, we predicted that GroEL, in which the 307‒309th amino acid residues were mutated to Ala, could alter the orientation of bound AC in GroEL. The GroEL-mediated photocyclodimerization of AC can be used for regioselective inversion upon ATP addition to a moderate extent.
GroEL 是一种伴侣蛋白，负责肽和变性蛋白的折叠，在折叠过程中，ATP 的结合和水解会导致其构象发生显著变化。利用这些构象变化，我们利用 GroEL 介导的 2-蒽羧酸（AC）的区域选择性光环二聚反应，以 ATP 水解作为外部刺激。我们设计并制备了最佳的 GroEL 突变体，用于近年来广泛应用的对接模拟。基于 AC 与 GroEL 突变体之间氢键模式与野生型之间的巨大差异，我们预测 GroEL 中第 307-309 位氨基酸残基突变为丙氨酸，可改变结合在 GroEL 中的 AC 的方向。GroEL 介导的 AC 光环二聚反应可以在一定程度上通过添加 ATP 进行区域选择性反转。
