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3agp

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Structure of viral polymerase form I

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 <StructureSection load='3agp' size='340' side='right'caption='[[3agp]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3agp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AGP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3agp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7], [https://en.wikipedia.org/wiki/Escherichia_virus_Qbeta Escherichia virus Qbeta] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AGP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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]] 2.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3agq|3agq]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=3agp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3agp OCA], [https://pdbe.org/3agp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3agp RCSB], [https://www.ebi.ac.uk/pdbsum/3agp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3agp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/EFTS_ECO57 EFTS_ECO57]] Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity).
+[https://www.uniprot.org/uniprot/EFTU_ECO57 EFTU_ECO57] [https://www.uniprot.org/uniprot/EFTS_ECO57 EFTS_ECO57] Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity).[https://www.uniprot.org/uniprot/RDRP_BPQBE RDRP_BPQBE] This enzyme is part of the viral RNA-dependent RNA polymerase complex.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Replication and transcription of viral RNA genomes rely on host-donated proteins. Qbeta virus infects Escherichia coli and replicates and transcribes its own genomic RNA by Qbeta replicase. Qbeta replicase requires the virus-encoded RNA-dependent RNA polymerase (beta-subunit), and the host-donated translational elongation factors EF-Tu and -Ts, as active core subunits for its RNA polymerization activity. Here, we present the crystal structure of the core Qbeta replicase, comprising the beta-subunit, EF-Tu and -Ts. The beta-subunit has a right-handed structure, and the EF-Tu:Ts binary complex maintains the structure of the catalytic core crevasse of the beta-subunit through hydrophobic interactions, between the finger and thumb domains of the beta-subunit and domain-2 of EF-Tu and the coiled-coil motif of EF-Ts, respectively. These hydrophobic interactions are required for the expression and assembly of the Qbeta replicase complex. Thus, EF-Tu and -Ts have chaperone-like functions in the maintenance of the structure of the active Qbeta replicase. Modeling of the template RNA and the growing RNA in the catalytic site of the Qbeta replicase structure also suggests that structural changes of the RNAs and EF-Tu:Ts should accompany processive RNA polymerization and that EF-Tu:Ts in the Qbeta replicase could function to modulate the RNA folding and structure.
-Assembly of Q{beta} viral RNA polymerase with host translational elongation factors EF-Tu and -Ts.,Takeshita D, Tomita K Proc Natl Acad Sci U S A. 2010 Sep 7;107(36):15733-8. Epub 2010 Aug 23. PMID:20798060<ref>PMID:20798060</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3agp" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Elongation factor 3D structures|Elongation factor 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
+[[Category: Escherichia coli O157:H7]]
+[[Category: Escherichia virus Qbeta]]
 [[Category: Large Structures]]
-[[Category: Takeshita, D]]
+[[Category: Synthetic construct]]
-[[Category: Tomita, K]]
+[[Category: Takeshita D]]
-[[Category: Replicase]]
+[[Category: Tomita K]]
-[[Category: Rna polymerase]]
-[[Category: Transferase]]
-[[Category: Translation]]

3agp

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Structure of viral polymerase form I

Structural highlights

Function

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