2uuw: Difference between revisions

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-[[Image:2uuw.jpg|left|200px]]<br /><applet load="2uuw" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2uuw, resolution 2.76&Aring;" />
-'''2.75 ANGSTROM STRUCTURE OF THE D347G D348G MUTANT STRUCTURE OF SAPPORO VIRUS RDRP POLYMERASE'''<br />
-==About this Structure==
+==2.75 angstrom structure of the D347G D348G mutant structure of Sapporo Virus RdRp Polymerase==
-UUW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caliciviridae Caliciviridae]. Active as [http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UUW OCA].
+<StructureSection load='2uuw' size='340' side='right'caption='[[2uuw]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
-[[Category: Caliciviridae]]
+== Structural highlights ==
-[[Category: RNA-directed RNA polymerase]]
+<table><tr><td colspan='2'>[[2uuw]] 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=2UUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UUW FirstGlance]. <br>
-[[Category: Single protein]]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.76&#8491;</td></tr>
-[[Category: Fullerton, S.]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2uuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uuw OCA], [https://pdbe.org/2uuw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uuw RCSB], [https://www.ebi.ac.uk/pdbsum/2uuw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uuw ProSAT]</span></td></tr>
-[[Category: Gebhardt, J.]]
+</table>
-[[Category: Robel, I.]]
+== Function ==
-[[Category: Rohayem, J.]]
+[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).
-[[Category: Schuldt, L.]]
+== Evolutionary Conservation ==
-[[Category: Tucker, P.]]
+[[Image:Consurf_key_small.gif|200px|right]]
-[[Category: atp-binding]]
+Check<jmol>
-[[Category: capsid protein]]
+  <jmolCheckbox>
-[[Category: covalent protein-rna linkage]]
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uu/2uuw_consurf.spt"</scriptWhenChecked>
-[[Category: helicase]]
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-[[Category: hydrolase]]
+    <text>to colour the structure by Evolutionary Conservation</text>
-[[Category: mutant]]
+  </jmolCheckbox>
-[[Category: nucleotide-binding]]
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2uuw ConSurf].
-[[Category: nucleotidyltransferase]]
+<div style="clear:both"></div>
-[[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]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:50:27 2008''
+==See Also==
+*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Sapporo virus]]
+[[Category: Fullerton S]]
+[[Category: Gebhardt J]]
+[[Category: Robel I]]
+[[Category: Rohayem J]]
+[[Category: Schuldt L]]
+[[Category: Tucker P]]