View source for 6su3


==Crystal structure of the 48C12 heliorhodopsin in the violet form at pH 8.8==
<StructureSection load='6su3' size='340' side='right'caption='[[6su3]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6su3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinomycetia_bacterium Actinomycetia bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SU3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LFA:EICOSANE'>LFA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6su3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6su3 OCA], [https://pdbe.org/6su3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6su3 RCSB], [https://www.ebi.ac.uk/pdbsum/6su3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6su3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2R4S913_9ACTN A0A2R4S913_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rhodopsins are the most abundant light-harvesting proteins. A new family of rhodopsins, heliorhodopsins (HeRs), has recently been discovered. Unlike in the known rhodopsins, in HeRs the N termini face the cytoplasm. The function of HeRs remains unknown. We present the structures of the bacterial HeR-48C12 in two states at the resolution of 1.5 A, which highlight its remarkable difference from all known rhodopsins. The interior of HeR's extracellular part is completely hydrophobic, while the cytoplasmic part comprises a cavity (Schiff base cavity [SBC]) surrounded by charged amino acids and containing a cluster of water molecules, presumably being a primary proton acceptor from the Schiff base. At acidic pH, a planar triangular molecule (acetate) is present in the SBC. Structure-based bioinformatic analysis identified 10 subfamilies of HeRs, suggesting their diverse biological functions. The structures and available data suggest an enzymatic activity of HeR-48C12 subfamily and their possible involvement in fundamental redox biological processes.

High-resolution structural insights into the heliorhodopsin family.,Kovalev K, Volkov D, Astashkin R, Alekseev A, Gushchin I, Haro-Moreno JM, Chizhov I, Siletsky S, Mamedov M, Rogachev A, Balandin T, Borshchevskiy V, Popov A, Bourenkov G, Bamberg E, Rodriguez-Valera F, Buldt G, Gordeliy V Proc Natl Acad Sci U S A. 2020 Feb 7. pii: 1915888117. doi:, 10.1073/pnas.1915888117. PMID:32034096<ref>PMID:32034096</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6su3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Actinomycetia bacterium]]
[[Category: Large Structures]]
[[Category: Alekseev A]]
[[Category: Astashkin R]]
[[Category: Gordeliy V]]
[[Category: Gushchin I]]
[[Category: Kovalev K]]
[[Category: Volkov D]]