This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3avt

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 15:06, 29 December 2021

Structure of viral RNA polymerase complex 1

Structural highlights

3avt is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	3avu, 3avv, 3avw, 3avx, 3avy
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).

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.

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^[1]

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

References

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3avt"

@@ Line 3: / Line 3: @@
 <StructureSection load='3avt' size='340' side='right'caption='[[3avt]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3avt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AVT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AVT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3avt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AVT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AVT 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>, <scene name='pdbligand=GH3:3-DEOXY-GUANOSINE-5-TRIPHOSPHATE'>GH3</scene></td></tr>
+</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>, <scene name='pdbligand=GH3:3-DEOXY-GUANOSINE-5-TRIPHOSPHATE'>GH3</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3avu|3avu]], [[3avv|3avv]], [[3avw|3avw]], [[3avx|3avx]], [[3avy|3avy]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3avu|3avu]], [[3avv|3avv]], [[3avw|3avw]], [[3avx|3avx]], [[3avy|3avy]]</div></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=3avt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3avt OCA], [http://pdbe.org/3avt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3avt RCSB], [http://www.ebi.ac.uk/pdbsum/3avt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3avt ProSAT]</span></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=3avt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3avt OCA], [https://pdbe.org/3avt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3avt RCSB], [https://www.ebi.ac.uk/pdbsum/3avt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3avt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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).
+[[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).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3avt

From Proteopedia

Revision as of 15:06, 29 December 2021

Structure of viral RNA polymerase complex 1

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox