3avv: Difference between revisions

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~~{{STRUCTURE_3avv~~| ~~PDB~~=3avv | ~~SCENE~~= }}

==Structure of viral RNA polymerase complex 3==

===~~Structure~~ of viral RNA ~~polymerase complex~~ 3~~===~~

~~{{ABSTRACT_PUBMED_22245970}}~~

== Structural highlights ==

<table><tr><td colspan='2'>[[3avv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o157:h7 Escherichia coli o157:h7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AVV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AVV FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3avv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3avv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3avv RCSB], [http://www.ebi.ac.uk/pdbsum/3avv PDBsum]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Core Qbeta replicase comprises the Qbeta virus-encoded RNA-dependent RNA polymerase (beta-subunit) and the host Escherichia coli translational elongation factors EF-Tu and EF-Ts. The functions of the host proteins in the viral replicase are not clear. Structural analyses of RNA polymerization by core Qbeta replicase reveal that at the initiation stage, the 3'-adenine of the template RNA provides a stable platform for de novo initiation. EF-Tu in Qbeta replicase forms a template exit channel with the beta-subunit. At the elongation stages, the C-terminal region of the beta-subunit, assisted by EF-Tu, splits the temporarily double-stranded RNA between the template and nascent RNAs before translocation of the single-stranded template RNA into the exit channel. Therefore, EF-Tu in Qbeta replicase modulates RNA elongation processes in a distinct manner from its established function in protein synthesis.

~~==Function==~~

Molecular basis for RNA polymerization by Qbeta replicase.,Takeshita D, Tomita K Nat Struct Mol Biol. 2012 Jan 15;19(2):229-37. doi: 10.1038/nsmb.2204. PMID:22245970<ref>PMID:22245970</ref>

~~[[http://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)~~.

~~==About this Structure==~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

~~[[3avv]] is~~ a ~~3 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Escherichia_coli_o157:h7 Escherichia coli o157:h7]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3AVV OCA].~~

</div>

== References ==

==~~Reference~~==

~~<ref group="xtra">PMID:022245970</ref>~~<references ~~group="xtra"~~/><~~references~~/>

__TOC__

</StructureSection>

[[Category: Escherichia coli o157:h7]]

[[Category: Takeshita, D.]]

[[Category: Takeshita, D]]

[[Category: Tomita, K.]]

[[Category: Tomita, K]]

[[Category: Rna polymerase]]

[[Category: Transferase-rna complex]]

[[Category: Translation]]

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@@ Line 1: / Line 1: @@
-{{STRUCTURE_3avv|  PDB=3avv  |  SCENE=  }}
+==Structure of viral RNA polymerase complex 3==
-===Structure of viral RNA polymerase complex 3===
+<StructureSection load='3avv' size='340' side='right' caption='[[3avv]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
-{{ABSTRACT_PUBMED_22245970}}
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3avv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o157:h7 Escherichia coli o157:h7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AVV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AVV FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3avt|3avt]], [[3avu|3avu]], [[3avw|3avw]], [[3avx|3avx]], [[3avy|3avy]]</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3avv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3avv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3avv RCSB], [http://www.ebi.ac.uk/pdbsum/3avv PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Core Qbeta replicase comprises the Qbeta virus-encoded RNA-dependent RNA polymerase (beta-subunit) and the host Escherichia coli translational elongation factors EF-Tu and EF-Ts. The functions of the host proteins in the viral replicase are not clear. Structural analyses of RNA polymerization by core Qbeta replicase reveal that at the initiation stage, the 3'-adenine of the template RNA provides a stable platform for de novo initiation. EF-Tu in Qbeta replicase forms a template exit channel with the beta-subunit. At the elongation stages, the C-terminal region of the beta-subunit, assisted by EF-Tu, splits the temporarily double-stranded RNA between the template and nascent RNAs before translocation of the single-stranded template RNA into the exit channel. Therefore, EF-Tu in Qbeta replicase modulates RNA elongation processes in a distinct manner from its established function in protein synthesis.
-==Function==
+Molecular basis for RNA polymerization by Qbeta replicase.,Takeshita D, Tomita K Nat Struct Mol Biol. 2012 Jan 15;19(2):229-37. doi: 10.1038/nsmb.2204. PMID:22245970<ref>PMID:22245970</ref>
-[[http://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).
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[3avv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o157:h7 Escherichia coli o157:h7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AVV OCA].
+</div>
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:022245970</ref><references group="xtra"/><references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli o157:h7]]
-[[Category: Takeshita, D.]]
+[[Category: Takeshita, D]]
-[[Category: Tomita, K.]]
+[[Category: Tomita, K]]
 [[Category: Rna polymerase]]
 [[Category: Transferase-rna complex]]
 [[Category: Translation]]