View source for 9ljj


==cryo-EM structure of a nanobody bound heliorhodopsin==
<StructureSection load='9ljj' size='340' side='right'caption='[[9ljj]], [[Resolution|resolution]] 3.23&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ljj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Vicugna_pacos Vicugna pacos]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9LJJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9LJJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.23&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=PX2:1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE'>PX2</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9ljj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ljj OCA], [https://pdbe.org/9ljj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ljj RCSB], [https://www.ebi.ac.uk/pdbsum/9ljj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ljj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2R4S913_9ACTN A0A2R4S913_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

Cryo-EM structure of a nanobody-bound heliorhodopsin.,Xia R, Sun M, Lu Y, Wang N, Zhang A, Guo C, Xu Z, Cai X, He Y Biochem Biophys Res Commun. 2025 Mar 1;750:151398. doi: , 10.1016/j.bbrc.2025.151398. Epub 2025 Jan 25. PMID:39889627<ref>PMID:39889627</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9ljj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Vicugna pacos]]
[[Category: He Y]]
[[Category: Xia R]]