2ckw: Difference between revisions

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 <StructureSection load='2ckw' size='340' side='right'caption='[[2ckw]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ckw]] is a 1 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=2CKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CKW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ckw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sapporo_virus Sapporo virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CKW FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span></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]] 2.3&#8491;</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=2ckw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ckw OCA], [https://pdbe.org/2ckw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ckw RCSB], [https://www.ebi.ac.uk/pdbsum/2ckw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ckw ProSAT]</span></td></tr>
 </table>
 == 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).
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 __TOC__
 </StructureSection>
-[[Category: Human calicivirus slv]]
 [[Category: Large Structures]]
-[[Category: RNA-directed RNA polymerase]]
+[[Category: Sapporo virus]]
-[[Category: Canard, B]]
+[[Category: Canard B]]
-[[Category: Coutard, B]]
+[[Category: Coutard B]]
-[[Category: Fullerton, S W.B]]
+[[Category: Fullerton SWB]]
-[[Category: Gebhardt, J]]
+[[Category: Gebhardt J]]
-[[Category: Gorbalenya, A]]
+[[Category: Gorbalenya A]]
-[[Category: Rohayem, J]]
+[[Category: Rohayem J]]
-[[Category: Tucker, P A]]
+[[Category: Tucker PA]]
-[[Category: Atp-binding]]
-[[Category: Capsid protein]]
-[[Category: Covalent protein-rna linkage]]
-[[Category: Helicase]]
-[[Category: Hydrolase]]
-[[Category: Mutant]]
-[[Category: Nucleotide-binding]]
-[[Category: Nucleotidyltransferase]]
-[[Category: Polymerase]]
-[[Category: Polyprotein]]
-[[Category: Protease]]
-[[Category: Rna elongation]]
-[[Category: Rna replication]]
-[[Category: Rna-directed rna polymerase]]
-[[Category: Structural protein]]
-[[Category: Thiol protease]]
-[[Category: Transferase]]
-[[Category: Transferase activity]]