7clj
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='7clj' size='340' side='right'caption='[[7clj]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='7clj' size='340' side='right'caption='[[7clj]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CLJ 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]] 2.6Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=7clj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7clj OCA], [https://pdbe.org/7clj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7clj RCSB], [https://www.ebi.ac.uk/pdbsum/7clj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7clj ProSAT]</span></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=7clj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7clj OCA], [https://pdbe.org/7clj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7clj RCSB], [https://www.ebi.ac.uk/pdbsum/7clj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7clj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/A0A151EDA9_9ARCH A0A151EDA9_9ARCH] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Microbial rhodopsins comprise an opsin protein with seven transmembrane helices and a retinal as the chromophore. An all-trans retinal is covalently bonded to a lysine residue through the retinal Schiff base (RSB) and stabilized by a negatively charged counterion. The distance between the RSB and counterion is closely related to the light energy absorption. However, in heliorhodopsin-48C12 (HeR-48C12), while E107 acts as the counterion, E107D mutation exhibits an identical absorption spectrum to the wild-type, suggesting that the distance does not affect its absorption spectra. Here we present the 2.6 A resolution crystal structure of the Thermoplasmatales archaeon HeR E108D mutant, which also has an identical absorption spectrum to the wild-type. The structure revealed that D108 does not form a hydrogen bond with the RSB, and its counterion interaction becomes weaker. Alternatively, the serine cluster, S78, S112, and S238 form a distinct interaction network around the RSB. The absorption spectra of the E to D and S to A double mutants suggested that S112 influences the spectral shift by compensating for the weaker counterion interaction. Our structural and spectral studies have revealed the unique spectral shift mechanism of HeR and clarified the physicochemical properties of HeRs. | ||
| - | |||
| - | Structural basis for unique color tuning mechanism in heliorhodopsin.,Tanaka T, Singh M, Shihoya W, Yamashita K, Kandori H, Nureki O Biochem Biophys Res Commun. 2020 Sep 18. pii: S0006-291X(20)31342-5. doi:, 10.1016/j.bbrc.2020.06.124. PMID:32951839<ref>PMID:32951839</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 7clj" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Thermoplasmatales archaeon SG8-52-1]] | ||
[[Category: Nureki O]] | [[Category: Nureki O]] | ||
[[Category: Shihoya W]] | [[Category: Shihoya W]] | ||
[[Category: Tanaka T]] | [[Category: Tanaka T]] | ||
[[Category: Yamashita K]] | [[Category: Yamashita K]] | ||
Current revision
Crystal structure of Thermoplasmatales archaeon heliorhodopsin E108D mutant
| |||||||||||
