2wk4
From Proteopedia
(Difference between revisions)
Line 3: | Line 3: | ||
<StructureSection load='2wk4' size='340' side='right'caption='[[2wk4]], [[Resolution|resolution]] 2.98Å' scene=''> | <StructureSection load='2wk4' size='340' side='right'caption='[[2wk4]], [[Resolution|resolution]] 2.98Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2wk4]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2wk4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_calicivirus_slv Human calicivirus slv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WK4 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </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></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ckw|2ckw]], [[2uut|2uut]], [[2uuw|2uuw]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ckw|2ckw]], [[2uut|2uut]], [[2uuw|2uuw]]</div></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Calicivirin Calicivirin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.66 3.4.22.66] </span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wk4 OCA], [https://pdbe.org/2wk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wk4 RCSB], [https://www.ebi.ac.uk/pdbsum/2wk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wk4 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/POLG_SVM93 POLG_SVM93]] NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity (By similarity). Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation (By similarity). Protease-polymerase processes the polyprotein: Pro-Pol is first released by autocleavage, then all other proteins are cleaved (By similarity). Protease-polymerase is a RNA-directed RNA polymerase which replicates genomic and antigenomic viral RNA by recognizing specific signals. Catalyzes the covalent attachment VPg with viral RNAs (By similarity). Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells, inducing endocytosis of the viral particle. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm (By similarity). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 23: | Line 23: | ||
==See Also== | ==See Also== | ||
- | *[[RNA polymerase|RNA polymerase]] | + | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 10:55, 7 July 2021
Dimeric structure of D347G D348G mutant of the sapporovirus RNA dependent RNA polymerase
|
Categories: Calicivirin | Human calicivirus slv | Large Structures | Fullerton, S W.B | Gebhardt, J | Robel, I | Rohayem, J | Schuldt, L | Tucker, P A | Atp-binding | Capsid protein | Covalent protein-rna linkage | Helicase | Hydrolase | Nucleotidyltransferase | Phosphorylation | Protease | Rna elongation | Rna replication | Thiol protease