文献类型： 外文期刊
作者： Xia, Ruixue 1 ; Sun, Mingxia 2 ; Lu, Yang 1 ; Wang, Na 1 ; Zhang, Anqi 1 ; Guo, Changyou 1 ; Xu, Zhenmei 1 ; Cai, Xuehui 2 ; He, Yuanzheng 1 ;
作者机构： 1.Harbin Inst Technol, Fac Life Sci & Med, HIT Ctr Life Sci, Sch Life Sci & Technol, Harbin 150001, Peoples R China
2.Chinese Acad Agr Sci, State Key Lab Vet Biotechnol, Harbin Vet Res Inst, Harbin 150001, Peoples R China
3.Harbin Inst Technol, Frontiers Sci Ctr Matter Behave Space Environm, Harbin 150001, Peoples R China
关键词： Heliorhodopsin; Acetate; Nanobody; Cryo-EM
期刊名称：BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS （ 影响因子：2.2； 五年影响因子：2.5 ）
ISSN： 0006-291X
年卷期： 2025 年 750 卷
页码：
收录情况： SCI
摘要： Heliorhodopsins (HeRs) represent a distinct class of microbial rhodopsins (MRs) with an inverted membrane topology compared to other MRs. Previous structural studies have shown that HeRs lack a proton acceptor residue, and protons are never released from the protein. In this study, we present the cryo-electron microscopy (cryo-EM) structure of HeR bound to a nanobody. The structure reveals an acetate-like molecule in the Schiff base cavity (SBC) on the intracellular side of HeR under neutral condition. Structural comparisons and analyses suggest that the acetate molecule may function as a proton acceptor for the protonated retinal Schiff base (RSB) and act as a mediator for the intramolecular signaling transduction in HeR during light stimulation. These structural insights shed new light on the mechanism and function of HeR.
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