8tc5
From Proteopedia
(Difference between revisions)
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<StructureSection load='8tc5' size='340' side='right'caption='[[8tc5]], [[Resolution|resolution]] 2.11Å' scene=''> | <StructureSection load='8tc5' size='340' side='right'caption='[[8tc5]], [[Resolution|resolution]] 2.11Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[8tc5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[8tc5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Civet_SARS_CoV_SZ3/2003 Civet SARS CoV SZ3/2003]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8TC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TC5 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]] 2.11Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.11Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EIC:LINOLEIC+ACID'>EIC</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EIC:LINOLEIC+ACID'>EIC</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=8tc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8tc5 OCA], [https://pdbe.org/8tc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8tc5 RCSB], [https://www.ebi.ac.uk/pdbsum/8tc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8tc5 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=8tc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8tc5 OCA], [https://pdbe.org/8tc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8tc5 RCSB], [https://www.ebi.ac.uk/pdbsum/8tc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8tc5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | SARS-CoV-2 is the third known coronavirus (CoV) that has crossed the animal-human barrier in the last two decades. However, little structural information exists related to the close genetic species within the SARS-related coronaviruses. Here, we present three novel SARS-related CoV spike protein structures solved by single particle cryo-electron microscopy analysis derived from bat (bat SL-CoV WIV1) and civet (cCoV-SZ3, cCoV-007) hosts. We report complex glycan trees that decorate the glycoproteins and density for water molecules which facilitated modeling of the water molecule coordination networks within structurally important regions. We note structural conservation of the fatty acid binding pocket and presence of a linoleic acid molecule which are associated with stabilization of the receptor binding domains in the "down" conformation. Additionally, the N-terminal biliverdin binding pocket is occupied by a density in all the structures. Finally, we analyzed structural differences in a loop of the receptor binding motif between coronaviruses known to infect humans and the animal coronaviruses described in this study, which regulate binding to the human angiotensin converting enzyme 2 receptor. This study offers a structural framework to evaluate the close relatives of SARS-CoV-2, the ability to inform pandemic prevention, and aid in the development of pan-neutralizing treatments. | ||
| + | |||
| + | Variation in structural motifs within SARS-related coronavirus spike proteins.,Hills FR, Eruera AR, Hodgkinson-Bean J, Jorge F, Easingwood R, Brown SHJ, Bouwer JC, Li YP, Burga LN, Bostina M PLoS Pathog. 2024 May 28;20(5):e1012158. doi: 10.1371/journal.ppat.1012158. PMID:38805567<ref>PMID:38805567</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8tc5" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Civet SARS CoV SZ3/2003]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Paguma larvata]] | ||
[[Category: Bostina M]] | [[Category: Bostina M]] | ||
[[Category: Eruera A]] | [[Category: Eruera A]] | ||
[[Category: Hills FR]] | [[Category: Hills FR]] | ||
Current revision
Cryo-EM Structure of Spike Glycoprotein from Civet Coronavirus SZ3 in Closed Conformation
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