9LJJ
cryo-EM structure of a nanobody bound heliorhodopsin
Summary for 9LJJ
| Entry DOI | 10.2210/pdb9ljj/pdb |
| EMDB information | 63157 |
| Descriptor | Heliorhodopsin, nanobody B4, RETINAL, ... (6 entities in total) |
| Functional Keywords | bacterial rhodopsin, membrane protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 84623.82 |
| Authors | |
| Primary citation | Xia, R.,Sun, M.,Lu, Y.,Wang, N.,Zhang, A.,Guo, C.,Xu, Z.,Cai, X.,He, Y. Cryo-EM structure of a nanobody-bound heliorhodopsin. Biochem.Biophys.Res.Commun., 750:151398-151398, 2025 Cited by PubMed Abstract: 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. PubMed: 39889627DOI: 10.1016/j.bbrc.2025.151398 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.23 Å) |
Structure validation
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